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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P11979 | KPYM_FELCA | MSKPHSDVGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVEILKEMIKSGMNVARLNFSHGTHEYHAETIKNVRAATESFASDPIRYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENVLWLDYKNICKVVEVGSKVYVDDGLISLLVKEKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRA... | 2.7.1.40; 2.7.10.2; 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14618}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P14618}; | cellular response to insulin stimulus [GO:0032869]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of sprouting angiogenesis [GO:1903672] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; rough endoplasmic reticulum [GO:0005791] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; mRNA binding [GO:0003729]; potassium ion binding [GO:0030955]; protein tyrosine kinase activity [GO:0004713]; pyruvate kinase activity [GO:0004743] | PF00224;PF02887; | 3.20.20.60;2.40.33.10;3.40.1380.20; | Pyruvate kinase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P14618}.; PTM: Under hypoxia, hydroxylated by EGLN3. {ECO:0000250|UniProtKB:P14618}.; PTM: Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy. {ECO:00002... | SUBCELLULAR LOCATION: [Isoform M2]: Cytoplasm {ECO:0000250|UniProtKB:P14618}. Nucleus {ECO:0000250|UniProtKB:P14618}. Note=Translocates to the nucleus in response to various signals, such as EGF receptor activation or apoptotic stimuli. {ECO:0000250|UniProtKB:P14618}.; SUBCELLULAR LOCATION: [Isoform M1]: Cytoplasm {ECO... | CATALYTIC ACTIVITY: [Isoform M2]: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000250|UniProtKB:P14618}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:1... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. {ECO:0000250|UniProtKB:P14618}. | null | null | FUNCTION: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic proc... | Felis catus (Cat) (Felis silvestris catus) |
P11980 | KPYM_RAT | MPKPDSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIGPASRSVEMLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRAATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKEKGADYLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKAADVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRA... | 2.7.1.40; 2.7.10.2; 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14618}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P14618}; | animal organ regeneration [GO:0031100]; canonical glycolysis [GO:0061621]; cellular response to insulin stimulus [GO:0032869]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; liver development [GO:0001889]; phosphorylation [GO:0016310]; positive regulation of cytoplasmic translation [GO:2000767... | cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; pyruvate kinase complex [GO:1902912]; rough endoplasmic reticulum [GO:0005791] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; mRNA binding [GO:0003729]; potassium ion binding [GO:0030955]; protein dimerization activity [GO:0046983]; protein tyrosine kinase activity [GO:0004713]; pyruvate kinase activity [GO:0004743];... | PF00224;PF02887; | 3.20.20.60;2.40.33.10;3.40.1380.20; | Pyruvate kinase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P14618}.; PTM: Under hypoxia, hydroxylated by EGLN3. {ECO:0000250|UniProtKB:P14618}.; PTM: Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy. {ECO:00002... | SUBCELLULAR LOCATION: [Isoform M2]: Cytoplasm {ECO:0000250|UniProtKB:P14618}. Nucleus {ECO:0000250|UniProtKB:P14618}. Note=Translocates to the nucleus in response to various signals, such as EGF receptor activation or apoptotic stimuli. {ECO:0000250|UniProtKB:P14618}.; SUBCELLULAR LOCATION: [Isoform M1]: Cytoplasm {ECO... | CATALYTIC ACTIVITY: [Isoform M2]: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000250|UniProtKB:P14618}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:1... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. {ECO:0000250|UniProtKB:P14618}. | null | null | FUNCTION: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic proc... | Rattus norvegicus (Rat) |
P11983 | TCPA_MOUSE | MEGPLSVFGDRSTGEAVRSQNVMAAASIANIVKSSFGPVGLDKMLVDDIGDVTITNDGATILKLLEVEHPAAKVLCELADLQDKEVGDGTTSVVIIAAELLKNADELVKQKIHPTSVISGYRLACKEAVRYINENLIINTDELGRDCLINAAKTSMSSKIIGINGDYFANMVVDAVLAVKYTDARGQPRYPVNSVNILKAHGRSQIESMLINGYALNCVVGSQGMPKRIVNAKIACLDFSLQKTKMKLGVQVVITDPEKLDQIRQRESDITKERIQKILATGANVILTTGGIDDMYLKYFVEAGAMAVRRVLKRDLKHVA... | null | null | binding of sperm to zona pellucida [GO:0007339]; chaperone-mediated protein folding [GO:0061077]; positive regulation of establishment of protein localization to telomere [GO:1904851]; positive regulation of telomerase RNA localization to Cajal body [GO:1904874]; positive regulation of telomere maintenance via telomera... | acrosomal vesicle [GO:0001669]; cell body [GO:0044297]; centrosome [GO:0005813]; chaperonin-containing T-complex [GO:0005832]; Golgi apparatus [GO:0005794]; heterochromatin [GO:0000792]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; myelin sheath [GO:0043209]; pericentriolar material [GO:0000242... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; ubiquitin protein ligase binding [GO:0031625]; unfolded protein binding [GO:0051082] | PF00118; | 3.50.7.10;1.10.560.10;3.30.260.10; | TCP-1 chaperonin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P17987}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P17987}. | null | null | null | null | null | FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome... | Mus musculus (Mouse) |
P11985 | DYLT2_MOUSE | MERRGRMAKTPTGQTHQSPVSKRERKPSMFEKESYAQILRERLRESFHDVQYVEPPFDDSIADVGKEWKSALAKLKFANSYRMEPLKKFQAHLVETKIQQILKDSLKDVKYDDKAPHLSLELADGILAAVKEFAYHRYKFIIQVLFIQKTGQAINIASRWIWDVAWDNWVEAKHETESYVVLALVFALYCE | null | null | microtubule-based movement [GO:0007018] | cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule [GO:0005874]; sperm flagellum [GO:0036126] | dynein intermediate chain binding [GO:0045505] | PF03645; | 3.30.1140.40; | Dynein light chain Tctex-type family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:7601308}. Cytoplasmic granule {ECO:0000269|PubMed:7601308}. Membrane {ECO:0000269|PubMed:7601308}; Peripheral membrane protein {ECO:0000269|PubMed:7601308}. Note=Found on the surface of sperm tail. Stored in cytoplasmic granules during spermatogenesis. | null | null | null | null | null | FUNCTION: May be an accessory component of axonemal dynein and cytoplasmic dynein 1. Candidate for involvement in male sterility. {ECO:0000269|PubMed:11278908}. | Mus musculus (Mouse) |
P11986 | INO1_YEAST | MTEDNIAPITSVKVVTDKCTYKDNELLTKYSYENAVVTKTASGRFDVTPTVQDYVFKLDLKKPEKLGIMLIGLGGNNGSTLVASVLANKHNVEFQTKEGVKQPNYFGSMTQCSTLKLGIDAEGNDVYAPFNSLLPMVSPNDFVVSGWDINNADLYEAMQRSQVLEYDLQQRLKAKMSLVKPLPSIYYPDFIAANQDERANNCINLDEKGNVTTRGKWTHLQRIRRDIQNFKEENALDKVIVLWTANTERYVEVSPGVNDTMENLLQSIKNDHEEIAPSTIFAAASILEGVPYINGSPQNTFVPGLVQLAEHEGTFIAGDD... | 5.5.1.4 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:11779862, ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703, ECO:0000269|PubMed:14684747, ECO:0000269|Ref.6}; | inositol biosynthetic process [GO:0006021]; phospholipid biosynthetic process [GO:0008654] | cytoplasm [GO:0005737] | inositol-3-phosphate synthase activity [GO:0004512] | PF01658;PF07994; | 3.40.50.720; | Myo-inositol 1-phosphate synthase family | PTM: Phosphorylation at Ser-184 and Ser-374 is associated with a decrease in activity (PubMed:23902760). Increasingly phosphorylated in presence of valproate (PubMed:23902760). {ECO:0000269|PubMed:23902760}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate; Xref=Rhea:RHEA:10716, ChEBI:CHEBI:58401, ChEBI:CHEBI:61548; EC=5.5.1.4; Evidence={ECO:0000269|PubMed:14684747, ECO:0000269|PubMed:23902760, ECO:0000269|Ref.6, ECO:0000269|Ref.8}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 mM for D-glucose 6-phosphate (at 37 degrees Celsius and pH 7.2) {ECO:0000269|Ref.6}; KM=17 uM for NAD (at 37 degrees Celsius and pH 7.2) {ECO:0000269|Ref.6}; | PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-7.7. {ECO:0000269|PubMed:14684747}; | null | FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (PubMed:14684747, PubMed:23902760, Ref.6, Ref.8). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). {ECO:000025... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P11998 | RISB_BACSU | MNIIQGNLVGTGLKIGIVVGRFNDFITSKLLSGAEDALLRHGVDTNDIDVAWVPGAFEIPFAAKKMAETKKYDAIITLGTVIRGATTHYDYVCNEAAKGIAQAANTTGVPVIFGIVTTENIEQAIERAGTKAGNKGVDCAVSAIEMANLNRSFE | 2.5.1.78 | null | riboflavin biosynthetic process [GO:0009231] | cytosol [GO:0005829]; riboflavin synthase complex [GO:0009349] | 6,7-dimethyl-8-ribityllumazine synthase activity [GO:0000906] | PF00885; | 3.40.50.960; | DMRL synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78; Evid... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 uM for 5-amino-6-(D-ribitylamino)uracil {ECO:0000269|PubMed:12581640, ECO:0000269|PubMed:7893702}; KM=9 uM for 5-amino-6-(D-ribitylamino)uracil {ECO:0000269|PubMed:12581640, ECO:0000269|PubMed:7893702}; KM=130 uM for (3S)-3,4-dihydroxy-2-butanone 4-phosphate {ECO... | PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. {ECO:0000269|PubMed:7893702}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-8.0. {ECO:0000269|PubMed:7893702}; | null | FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. Is able to use the non-natural R enantiomer of 3,4-dihydroxy-2-butanone 4-phosphate as a subs... | Bacillus subtilis (strain 168) |
P12000 | DNLI1_SCHPO | MRTVFSQIPRFKQVNQYIRMSTRQSDISNFFISSASHKSEHVEVSQSSSDSKNVDGRSTSEKRKVESVKLVDESKHNNHDDTGTQNVERENNIVSEAKKQKTLGSSSSSSDAVSSNNDSGASTPIPLPIKEPPLESNARNDKLKGHATFAEMVKAFTKIENTSKRLEIIDIMGTYFFGILRDHPSDLLACVYLSINKLGPDYSGLELGIGESIIMKAIGESTGQTLQQIKLSFHKVGDLGLVAQTSRQNQPTMFKPAALTIPFLFDSLKKIAQMSGNQSQNRKIGVIKRLLSSCEGAEPKYLIRALEGKLRLQLAEKTIL... | 6.5.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | base-excision repair [GO:0006284]; cell division [GO:0051301]; DNA biosynthetic process [GO:0071897]; DNA ligation [GO:0006266]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; lagging strand elongation [GO:0006273]; mitochondrial DNA metabolic process [GO:0032042]; nucleotide-excision repair [GO:0006289]; Oka... | mitochondrion [GO:0005739]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; DNA ligase activity [GO:0003909]; metal ion binding [GO:0046872] | PF04679;PF01068;PF04675; | 3.30.1490.70;1.10.3260.10;3.30.470.30;2.40.50.140; | ATP-dependent DNA ligase family | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135}; | null | null | null | null | FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P12003 | VINC_CHICK | MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVSAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVRAAQMLQADPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNTKSQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALALIDSKMNQAKGWLRDPNAPPGDAGEQAIRQILDEAGKAGELCAGKERRE... | null | null | adherens junction assembly [GO:0034333]; apical junction assembly [GO:0043297]; axon extension [GO:0048675]; cell adhesion [GO:0007155]; epithelial cell-cell adhesion [GO:0090136]; lamellipodium assembly [GO:0030032]; morphogenesis of an epithelium [GO:0002009]; protein localization to cell surface [GO:0034394]; regula... | actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; brush border [GO:0005903]; cell projection [GO:0042995]; cell-cell contact zone [GO:0044291]; cell-cell junction [GO:0005911]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; fascia adherens [GO:0005916]; focal adhesion [GO:0005... | actin filament binding [GO:0051015]; alpha-actinin binding [GO:0051393]; alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; dystroglycan binding [GO:0002162]; muscle alpha-actinin binding [GO:0051371]; protein homodimerization activity [GO:0042803]; scaffold protein bi... | PF01044; | 1.20.120.230;1.20.120.810; | Vinculin/alpha-catenin family | PTM: Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1134 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques. {ECO:0000269|PubMed:15229287}.; PTM: Acetylated; mainly by myristic acid but a... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20584916}; Peripheral membrane protein {ECO:0000305|PubMed:20584916}; Cytoplasmic side {ECO:0000305|PubMed:20584916}. Cell junction, adherens junction {ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20584916}. Cell junction, focal adhesion {ECO:0000269|PubMed:200... | null | null | null | null | null | FUNCTION: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. {ECO:0000269|PubMed:15229287, ECO:0000269|Pu... | Gallus gallus (Chicken) |
P12004 | PCNA_HUMAN | MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS | null | null | base-excision repair, gap-filling [GO:0006287]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to UV [GO:0034644]; cellular response to xenobiotic stimulus [GO:0071466]; epithelial cell differentiation [GO:0030855]; estrous cycle [GO:0044849]; heart development [GO:0007507]; leading strand elong... | centrosome [GO:0005813]; chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; extracellular exosome [GO:0070062]; male germ cell nucleus [GO:0001673]; nuclear body [GO:0016604]; nuclear lamina [GO:0005652]; nuclear replication fork [GO:00435... | chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; dinucleotide insertion or deletion binding [GO:0032139]; DNA polymerase binding [GO:0070182]; DNA polymerase processivity factor activity [GO:0030337]; enzyme binding [GO:0019899]; histone acetyltransferase binding [GO:0035035]; identical protein binding... | PF02747;PF00705; | 3.70.10.10; | PCNA family | PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA. {ECO:0000269|PubMed:17115032}.; PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation (Pu... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:24115439, ECO:0000269|PubMed:24939902}. Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage (PubMed:24939902). Forms nuclear foci representing sites of ongoing DNA replication and vary in morphology and number during S phase... | null | null | null | null | null | FUNCTION: Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand (PubMed:35585232). Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but no... | Homo sapiens (Human) |
P12007 | IVD_RAT | MATAVRLLGRRVSSWRLRPLPSPLAVPQRAHSMLPVDDDINGLNEEQKQLRHTISKFVQENLAPKAQEIDQSNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASAAVGLSYGAHSNLCINQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMRLKAEKKGDHYVLNGNKFWITNGPDADVLVVYAKTDLTAVPASRGITAFIVEKDMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANILSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQF... | 1.3.8.1; 1.3.8.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:6401713}; | branched-chain amino acid catabolic process [GO:0009083]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; leucine catabolic process [GO:0006552]; leucine metabolic process [GO:0006551] | mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | butyryl-CoA dehydrogenase activity [GO:0004085]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; isovaleryl-CoA dehydrogenase activity [GO:0008470] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:6401713}. | CATALYTIC ACTIVITY: Reaction=3-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = 3-methyl-(2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:12276, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57344, ChEBI:CHEBI:57345, ChEBI:CHEBI:57692, ChEB... | null | PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3. | null | null | FUNCTION: Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-C... | Rattus norvegicus (Rat) |
P12008 | AROC_ECOLI | MAGNTIGQLFRVTTFGESHGLALGCIVDGVPPGIPLTEADLQHDLDRRRPGTSRYTTQRREPDQVKILSGVFEGVTTGTSIGLLIENTDQRSQDYSAIKDVFRPGHADYTYEQKYGLRDYRGGGRSSARETAMRVAAGAIAKKYLAEKFGIEIRGCLTQMGDIPLDIKDWSQVEQNPFFCPDPDKIDALDELMRALKKEGDSIGAKVTVVASGVPAGLGEPVFDRLDADIAHALMSINAVKGVEIGDGFDVVALRGSQNRDEITKDGFQSNHAGGILGGISSGQQIIAHMALKPTSSITVPGRTINRFGEEVEMITKGRH... | 4.2.3.5 | COFACTOR: Name=FMNH2; Xref=ChEBI:CHEBI:57618; Evidence={ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:10956653, ECO:0000269|PubMed:11034781, ECO:0000269|PubMed:2969724, ECO:0000269|PubMed:7978236, ECO:0000269|PubMed:8824216, ECO:0000269|PubMed:9761730}; Note=Reduced FMN (FMNH(2)). It can also use FAD, however FMN... | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] | cytosol [GO:0005829] | chorismate synthase activity [GO:0004107]; FMN binding [GO:0010181]; identical protein binding [GO:0042802] | PF01264; | 3.60.150.10; | Chorismate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:10956653, ECO:0000269|PubMed:11034781, ECO:0000269|PubMed:7848266, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 uM for EPSP {ECO:0000269|PubMed:7978236}; Vmax=25 umol/min/mg enzyme {ECO:0000269|PubMed:7978236}; Note=kcat is 16.5 sec(-1) for phospholyase activity with EPSP as substrate. kcat is 27 sec(-1) for phospholyase activity with EPSP as substrate. {ECO:0000269|PubM... | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7.5 and 8. {ECO:0000269|PubMed:7978236}; | null | FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction intr... | Escherichia coli (strain K12) |
P12018 | VPREB_HUMAN | MSWAPVLLMLFVYCTGCGPQPVLHQPPAMSSALGTTIRLTCTLRNDHDIGVYSVYWYQQRPGHPPRFLLRYFSQSDKSQGPQVPPRFSGSKDVARNRGYLSISELQPEDEAMYYCAMGARSSEKEEREREWEEEMEPTAARTRVP | null | null | immune response [GO:0006955] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | null | PF07686; | 2.60.40.10; | Immunoglobulin superfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P13372}. | null | null | null | null | null | FUNCTION: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation. | Homo sapiens (Human) |
P12019 | PDE1_DICDI | MALNKKLISLLLLIFIILNIVNSHQQEDCDDDDEDIGISAERSERRSVKNSNDGSNFYNLNDYYTPENWNYYSGSFATKDCRDASYITIPLGTTGGLDEGNLSSFLLTKKGSNLFIALDAGTVWQGVRRLTTFKYFNTLFNITYPSWAVLPEQRTSWFLKNHVMSYFIGHSHLDHVGGLILVSPEDYLAKNWIDVQPPINNGIMGLIRKLGFKPTDFTSSSILQKKTIMGLPSTINSISTNLFNNQVWPNLPSFGRYQYFSLASGIEYPFTELVPYNATTMSLVANEFPFSVKVKPFELCHDNLISTSFLFTDSISGEQI... | 3.1.4.35; 3.1.4.53 | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; aggregation involved in sorocarp development [GO:0031152]; cAMP catabolic process [GO:0006198]; extracellular regulation of signal transduction [GO:1900115]; negative regulation of glucose mediated signaling pathway [GO:1902660]; re... | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; 3',5'-cyclic-nucleotide phosphodiesterase activity [GO:0004114]; cAMP binding [GO:0030552]; cGMP binding [GO:0030553] | PF02112; | 3.60.15.10; | Cyclic nucleotide phosphodiesterase class-II family | null | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:17040207}. Cell surface {ECO:0000269|PubMed:17040207}. | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:5774... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for cAMP {ECO:0000269|PubMed:12429832}; KM=1.8 uM for cGMP {ECO:0000269|PubMed:12429832}; Vmax=700 pmol/min/mg enzyme with cAMP as substrate {ECO:0000269|PubMed:12429832}; Vmax=490 pmol/min/mg enzyme with cGMP as substrate {ECO:0000269|PubMed:12429832}; Note... | null | null | null | FUNCTION: Phosphodiesterase which displays a preference for cAMP over cGMP. Involved in the degradation of extracellular cAMP. Maintains the responsiveness of cells to the chemoattractant cAMP during the aggregation phase of development. {ECO:0000269|PubMed:12429832}. | Dictyostelium discoideum (Social amoeba) |
P12023 | A4_MOUSE | MLPSLALLLLAAWTVRALEVPTDGNAGLLAEPQIAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDSVDSADAEEDDSDVWWGGADTDYADGGEDKVVEVAEEEEVADVEEEEADDDEDVEDGDEVEEEAEEPYEEATERTTSTATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCVPFF... | null | null | adult locomotory behavior [GO:0008344]; amyloid fibril formation [GO:1990000]; antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; astrocyte activation involved in immune response [GO:0002265]; axo-d... | apical part of cell [GO:0045177]; astrocyte projection [GO:0097449]; axon [GO:0030424]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; ciliary rootlet [GO:0035253]; clathrin-coated pit [GO:0005905]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:003... | growth factor receptor binding [GO:0070851]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; ion binding [GO:0043167]; peptidase activator activity [GO:0016504]; protein kinase binding [GO:0019901]; PTB domain binding [GO:0051425]; receptor ligand activity [GO:0048018]; RNA polymerase II cis-regul... | PF10515;PF12924;PF12925;PF02177;PF03494;PF00014; | 6.10.250.1670;1.20.120.770;3.30.1490.140;3.90.570.10;4.10.410.10;2.30.29.30; | APP family | PTM: Proteolytically processed under normal cellular conditions (PubMed:11553691, PubMed:23931995). Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchore... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26260791}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05067}. Membrane {ECO:0000250|UniProtKB:P05067}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05067}. Perikaryon {ECO:0000250|UniProtKB:P08592}. Cell projection, growth cone {ECO... | null | null | null | null | null | FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through pro... | Mus musculus (Mouse) |
P12024 | CHAO_DROME | MGLEFFFKFGYAFLTITLMIMIWMSLARASMFDREMEETHYPPCTYNVMCTCSKSSTDLGIVHCKNVPFPALPRMVNQSKVFMLHMENTGLREIEPYFLQSTGMYRLKISGNHLTEIPDDAFTGLERSLWELILPQNDLVEIPSKSLRHLQKLRHLDLGYNHITHIQHDSFRGLEDSLQTLILRENCISQLMSHSFSGLLILETLDLSGNNLFEIDPNVFVDGMPRLTRLLLTDNILSEIPYDALGPLKSLRTLDISHNVIWSLSGNETYEIKASTKLNLDNLHLEYNHIEVLPPNSFKYFDTVNRTFFDGNPIHTLRED... | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; microvillus organization [GO:0032528]; response to stimulus [GO:0050896]; rhabdomere development [GO:0042052]; visual perception [GO:0007601] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; rhabdomere [GO:0016028]; rhabdomere microvillus [GO:0035996] | null | PF00560;PF13855; | 3.80.10.10; | Chaoptin family | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side. Note=Extracellular surface of R-cell plasma membrane. | null | null | null | null | null | FUNCTION: Required for photoreceptor cell morphogenesis. Mediates homophilic cellular adhesion. {ECO:0000269|PubMed:19415110}. | Drosophila melanogaster (Fruit fly) |
P12025 | MK_MOUSE | MQHRGFFLLALLALLVVTSAVAKKKEKVKKGSECSEWTWGPCTPSSKDCGMGFREGTCGAQTQRVHCKVPCNWKKEFGADCKYKFESWGACDGSTGTKARQGTLKKARYNAQCQETIRVTKPCTSKTKSKTKAKKGKGKD | null | null | adrenal gland development [GO:0030325]; behavioral fear response [GO:0001662]; cell migration [GO:0016477]; cerebellar granular layer development [GO:0021681]; cerebral cortex development [GO:0021987]; cytoskeleton organization [GO:0007010]; defecation [GO:0030421]; dentate gyrus development [GO:0021542]; estrous cycle... | cell projection [GO:0042995]; extracellular region [GO:0005576] | chondroitin sulfate binding [GO:0035374]; growth factor activity [GO:0008083]; heparan sulfate binding [GO:1904399]; heparin binding [GO:0008201] | PF01091;PF05196; | 2.20.60.10; | Pleiotrophin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Secreted protein that functions as a cytokine and growth factor and mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors (PubMed:16901907). Binds cell-surface proteoglycan receptors via their chondroitin sulfate (CS) groups (PubMed:17230638). Thereby regulates many processes li... | Mus musculus (Mouse) |
P12026 | ACBP_PIG | MSQAEFEKAAEEVKNLKTKPADDEMLFIYSHYKQATVGDINTERPGILDLKGKAKWDAWNGLKGTSKEDAMKAYINKVEELKKKYGI | null | null | defense response to bacterium [GO:0042742]; fatty acid metabolic process [GO:0006631] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739] | fatty-acyl-CoA binding [GO:0000062] | PF00887; | 1.20.80.10; | ACBP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P07108}. Golgi apparatus {ECO:0000250|UniProtKB:P07108}. Note=Golgi localization is dependent on ligand binding. {ECO:0000250|UniProtKB:P07108}. | null | null | null | null | null | FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as... | Sus scrofa (Pig) |
P12032 | TIMP1_MOUSE | MMAPFASLASGILLLLSLIASSKACSCAPPHPQTAFCNSDLVIRAKFMGSPEINETTLYQRYKIKMTKMLKGFKAVGNAADIRYAYTPVMESLCGYAHKSQNRSEEFLITGRLRNGNLHISACSFLVPWRTLSPAQQRAFSKTYSAGCGVCTVFPCLSIPCKLESDTHCLWTDQVLVGSEDYQSRHFACLPRNPGLCTWRSLGAR | null | null | cartilage development [GO:0051216]; cellular response to UV-A [GO:0071492]; connective tissue replacement involved in inflammatory response wound healing [GO:0002248]; negative regulation of apoptotic process [GO:0043066]; negative regulation of catalytic activity [GO:0043086]; negative regulation of endopeptidase acti... | basement membrane [GO:0005604]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; metalloendopeptidase inhibitor activity [GO:0008191]; protease binding [GO:0002020]; zinc ion binding [GO:0008270] | PF00965; | 2.40.50.120;3.90.370.10; | Protease inhibitor I35 (TIMP) family | PTM: The activity of TIMP1 is dependent on the presence of disulfide bonds. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23522389}. | null | null | null | null | null | FUNCTION: Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP1... | Mus musculus (Mouse) |
P12034 | FGF5_HUMAN | MSLSFLLLLFFSHLILSAWAHGEKRLAPKGQPGPAATDRNPRGSSSRQSSSSAMSSSSASSSPAASLGSQGSGLEQSSFQWSPSGRRTGSLYCRVGIGFHLQIYPDGKVNGSHEANMLSVLEIFAVSQGIVGIRGVFSNKFLAMSKKGKLHASAKFTDDCKFRERFQENSYNTYASAIHRTEKTGREWYVALNKRGKAKRGCSPRVKPQHISTHFLPRFKQSEQPELSFTVTVPEKKKPPSPIKPKIPLSAPRKNTNSVKYRLKFRFG | null | null | animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cell-cell signaling [GO:0007267]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glial cell differentiation [GO:0010001]; nervous system development [GO:0007399]; positive regulation of cell division [GO:0051781]; positive re... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regres... | Homo sapiens (Human) |
P12035 | K2C3_HUMAN | MSRQASKTSGGGSQGFSGRSAVVSGSSRMSCVAHSGGAGGGAYGFRSGAGGFGSRSLYNLGGNKSISISVAAGGSRAGGFGGGRSSCAFAGGYGGGFGSGYGGGFGGGFGGGRGMGGGFGGAGGFGGAGGFGGAGGFGGPGGFGGSGGFGGPGSLGSPGGFGPGGFPGGIQEVTINQSLLQPLNVEIDPQIGQVKAQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWNLLQQQGTSSISGTNNLEPLFENHINYLRSYLDNILGERGRLDSELKNMEDLVEDFKKKYEDEINKRTAAENEFVTLKKDVDSAYMNKVE... | null | null | epithelial cell differentiation [GO:0030855]; intermediate filament cytoskeleton organization [GO:0045104]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095] | structural constituent of skin epidermis [GO:0030280] | PF00038;PF16208; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
P12036 | NFH_HUMAN | MMSFGGADALLGAPFAPLHGGGSLHYALARKGGAGGTRSAAGSSSGFHSWTRTSVSSVSASPSRFRGAGAASSTDSLDTLSNGPEGCMVAVATSRSEKEQLQALNDRFAGYIDKVRQLEAHNRSLEGEAAALRQQQAGRSAMGELYEREVREMRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDDEARQREEAEAAARALARFAQEAEAARVDLQKKAQALQEECGYLRRHHQEEVGELLGQIQGSGAAQAQMQAETRDALKCDVTSALREIRAQLEGHAVQSTLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITE... | null | null | axon development [GO:0061564]; axonogenesis [GO:0007409]; cell projection assembly [GO:0030031]; cellular response to leukemia inhibitory factor [GO:1990830]; intermediate filament bundle assembly [GO:0045110]; microtubule cytoskeleton organization [GO:0000226]; neurofilament bundle assembly [GO:0033693]; neurofilament... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; neurofibrillary tangle [GO:0097418]; neurofilament [GO:0005883]; postsynaptic density [GO:0014069]; postsynaptic intermediate filament cytoskeleton [GO:0099160]; Schaffer collateral - CA1 synapse [GO:0098685] | dynein complex binding [GO:0070840]; kinesin binding [GO:0019894]; microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of postsynaptic intermediate filament cytoskeleton [G... | PF07142;PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: There are a number of repeats of the tripeptide K-S-P, NFH is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFH results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber. {ECO:0000269|PubMed:8621664}.; PTM: Phosp... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27040688}. Cell projection, axon {ECO:0000250|UniProtKB:P19246}. | null | null | null | null | null | FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. NEFH has an important function in mature axons that is not subserved by the two smaller NF proteins. May additionally cooperate with the neuronal intermediate fi... | Homo sapiens (Human) |
P12041 | PURQ_BACSU | MKFAVIVLPGSNCDIDMYHAVKDELGHEVEYVWHEETSLDGFDGVLIPGGFSYGDYLRCGAIARFANIMPAVKQAAAEGKPVLGVCNGFQILQELGLLPGAMRRNKDLKFICRPVELIVQNDETLFTASYEKGESITIPVAHGEGNFYCDDETLATLKENNQIAFTYGSNINGSVSDIAGVVNEKGNVLGMMPHPERAVDELLGSADGLKLFQSIVKNWRETHVTTA | 3.5.1.2; 6.3.5.3 | null | 'de novo' IMP biosynthetic process [GO:0006189]; glutamine metabolic process [GO:0006541] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; glutaminase activity [GO:0004359]; phosphoribosylformylglycinamidine synthase activity [GO:0004642] | PF13507; | 3.40.50.880; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00421}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:4... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=181 uM for ATP (FGAM synthase activity at pH 7.2 and 37 degrees Celsius) {ECO:0000269|PubMed:15301530}; KM=507 uM for FGAR (FGAM synthase activity at pH 7.2 and 37 degrees Celsius) {ECO:0000269|PubMed:15301530}; KM=1.3 mM for glutamine (FGAM synthase activity at pH... | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00421}. | null | null | FUNCTION: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... | Bacillus subtilis (strain 168) |
P12042 | PURL_BACSU | MSLLLEPSKEQIKEEKLYQQMGVSDDEFALIESILGRLPNYTEIGIFSVMWSEHCSYKNSKPILRKFPTSGERVLQGPGEGAGIVDIGDNQAVVFKIESHNHPSALEPYQGAATGVGGIIRDVFSMGARPIAVLNSLRFGELTSPRVKYLFEEVVAGIAGYGNCIGIPTVGGEVQFDSSYEGNPLVNAMCVGLINHEDIKKGQAKGVGNTVMYVGAKTGRDGIHGATFASEEMSDSSEEKRSAVQVGDPFMEKLLLEACLEVIQCDALVGIQDMGAAGLTSSSAEMASKAGSGIEMNLDLIPQRETGMTAYEMMLSESQE... | 6.3.5.3 | null | 'de novo' IMP biosynthetic process [GO:0006189]; purine nucleotide biosynthetic process [GO:0006164] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; glutaminase activity [GO:0004359]; magnesium ion binding [GO:0000287]; phosphoribosylformylglycinamidine synthase activity [GO:0004642] | PF00586;PF02769;PF18072; | 3.90.650.10;3.30.1330.10; | FGAMS family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:4... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=181 uM for ATP (FGAM synthase activity at pH 7.2 and 37 degrees Celsius) {ECO:0000269|PubMed:15301530}; KM=398 uM for ATP (Glutamine amidotransferase activity at pH 7.2 and 37 degrees Celsius) {ECO:0000269|PubMed:15301530}; KM=507 uM for FGAR (FGAM synthase activit... | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00420}. | null | null | FUNCTION: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... | Bacillus subtilis (strain 168) |
P12047 | PUR8_BACSU | MIERYSRPEMSAIWTDENRFQAWLEVEILACEAWAELGVIPKEDVKVMRENASFDINRILEIEKDTRHDVVAFTRAVSESLGEERKWVHYGLTSTDVVDTALSYLLKQANDILLKDLERFVDIIKEKAKEHKYTVMMGRTHGVHAEPTTFGLKLALWHEEMKRNLERFKQAKAGIEVGKISGAVGTYANIDPFVEQYVCEKLGLKAAPISTQTLQRDRHADYMATLALIATSIEKFAVEIRGLQKSETREVEEFFAKGQKGSSAMPHKRNPIGSENMTGMARVIRGYMMTAYENVPLWHERDISHSSAERIILPDATIAL... | 4.3.2.2 | null | 'de novo' AMP biosynthetic process [GO:0044208]; 'de novo' IMP biosynthetic process [GO:0006189]; AMP biosynthetic process [GO:0006167] | cytosol [GO:0005829] | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity [GO:0070626]; N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity [GO:0004018] | PF10397;PF00206; | 1.10.40.30;1.20.200.10;1.10.275.10; | Lyase 1 family, Adenylosuccinate lyase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate; Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567, ChEBI:CHEBI:456215; EC=4.3.2.2; Evidence={ECO:0000269|PubMed:15182182}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854; Evidence={ECO:0000305|PubMed:15182182}; CATALYTIC A... | null | PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. | null | null | FUNCTION: Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-... | Bacillus subtilis (strain 168) |
P12063 | SYYM_NEUCR | MLLRTKALIRSGGSIAKYAAANPSCFILQRRGLRREFGPKYTAKINEAEENWQARAEAIKKGKKQNTWDLFEERGYVKDTAGTKEHIAELMRTRRIGAYVGIDPTAPSLHVGHLLPLMPLFWMYLEGYKAFTLIGGSTAKIGDPTGRLKSRDHLSSSDATMNMTKIHYQLKKLWENVDTQMRARGYEADWARKRGIVNNNHWWNKQPMLEVLRRVGHALRIGPMLSRDTVKNKMTQGDGVSFAEFTYPIMQGWDWFELFYQQGVQMQIGGSDQYGNIISGLEVVKAARESEPDPQERKYVTPKTALDECVGFTVPLLTDS... | 6.1.1.1 | null | Group I intron splicing [GO:0000372]; mRNA processing [GO:0006397]; positive regulation of RNA splicing [GO:0033120]; RNA folding [GO:0034337]; tRNA aminoacylation [GO:0043039]; tyrosyl-tRNA aminoacylation [GO:0006437] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; tyrosine-tRNA ligase activity [GO:0004831] | PF00579;PF16714; | 3.40.50.620;3.10.290.10;1.10.240.10; | Class-I aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706, Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442, ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1; | null | null | null | null | FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Has both an aminoacyl-tRNA synthetase activity and is involved in the splicing of group I introns. It acts in intron splicing by s... | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P12074 | CX6A1_HUMAN | MAVVGVSSVSRLLGRSRPQLGRPMSSGAHGEEGSARMWKTLTFFVALPGVAVSMLNVYLKSHHGEHERPEFIAYPHLRIRTKPFPWGDGNHTLFHNPHVNPLPTGYEDE | null | null | cellular respiration [GO:0045333]; generation of precursor metabolites and energy [GO:0006091]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | enzyme regulator activity [GO:0030234]; oxidoreductase activity [GO:0016491] | PF02046; | 4.10.95.10; | Cytochrome c oxidase subunit 6A family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P32799}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Homo sapiens (Human) |
P12080 | ITA2_DROME | MSGDSIHRRRMALHCPITSLILLLIAMSAHGYNIDLPSYVRFRQSSNSMFGFSIAMHKGRSGFYGNQNNVSLIVGAPKFDTSRYQQGVTEAGGVFKCSLNDDDCKLVPFDSKGNNRNVDKEVVDRKSYQWLGATVATGRDSDLVVACAPRYVFHTMTPSRAFRIDPVGTCFTSHNFEEFYEVSPCRTNNWGYHRQGSCQAGFSAAINGNGSRLFIGAPGSWYWQGQTYSIPPDAKFPFKPPLYQPFGTGGMASSHDVTRPENQVFSTSESASVNDDSYLGYSMVTGDFDGDRSEDVAIGMPRGGNLVGRIVVNRWNMANI... | null | null | apposition of dorsal and ventral imaginal disc-derived wing surfaces [GO:0007475]; axon guidance [GO:0007411]; axonal defasciculation [GO:0007414]; border follicle cell migration [GO:0007298]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-matrix adhe... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383] | extracellular matrix binding [GO:0050840]; integrin binding [GO:0005178]; protein heterodimerization activity [GO:0046982] | PF01839;PF08441;PF20805;PF20806;PF00357; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | PTM: The heavy-light chain cleavage site is either in 1230-1231, or 1233-1234, or 1243-1244. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein {ECO:0000269|PubMed:19035354}. Lateral cell membrane {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein {ECO:0000269|PubMed:19035354}. Basal cell membrane {ECO:0000269|PubMed:19035354}; Single-p... | null | null | null | null | null | FUNCTION: Alpha-PS2/beta-PS is a receptor for Tig, wb and Ten-m. Involved in the function and/or development of the olfactory system. {ECO:0000269|PubMed:10821184, ECO:0000269|PubMed:7924982, ECO:0000269|PubMed:7972082, ECO:0000269|PubMed:9660786}. | Drosophila melanogaster (Fruit fly) |
P12081 | HARS1_HUMAN | MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISF... | 6.1.1.21 | null | histidyl-tRNA aminoacylation [GO:0006427]; mitochondrial translation [GO:0032543]; translation [GO:0006412]; tRNA aminoacylation for protein translation [GO:0006418] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; histidine-tRNA ligase activity [GO:0004821]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723] | PF03129;PF13393;PF00458; | 3.40.50.800;1.10.287.10; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:F1Q5D5}. | CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for histidine {ECO:0000269|PubMed:29235198}; KM=0.872 uM for tRNA(His) {ECO:0000269|PubMed:29235198}; KM=44.2 uM for ATP {ECO:0000269|PubMed:29235198}; Note=kcat is 5.4 sec(-1) for aminoacylation of tRNA(His) (PubMed:29235198). kcat is 4.1 sec(-1) for histidin... | null | null | null | FUNCTION: Catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP) (PubMed:29235198). Plays a role in axon guidance (PubMed:26072516). {ECO:0000269|PubMed:26072516, ECO:0000269|PubMed:29235198}. | Homo sapiens (Human) |
P12104 | FABPI_HUMAN | MAFDSTWKVDRSENYDKFMEKMGVNIVKRKLAAHDNLKLTITQEGNKFTVKESSTFRNIEVVFELGVTFNYNLADGTELRGTWSLEGNKLIGKFKRTDNGNELNTVREIIGDELVQTYVYEGVEAKRIFKKD | null | null | fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; intestinal lipid absorption [GO:0098856] | apical cortex [GO:0045179]; cytosol [GO:0005829]; microvillus [GO:0005902]; nucleus [GO:0005634] | fatty acid binding [GO:0005504]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fat... | Homo sapiens (Human) |
P12105 | CO3A1_CHICK | MMSFVQKVSLFILAVFQPSVILAQQDALGGCTHLGQEYADRDVWKPEPCQICVCDSGSVLCDDIICDDQELDCPNPEIPLGECCPVCPQTTPQPTELPYTQGPKGDPGSPGSPGRTGAPGPPGQPGSPGAPGPPGICQSCPSISGGSFSPQYDSYDVKAGSVGMGYPPQPISGFPGPPGPSGPPGPPGHAGPPGSNGYQGPPGEPGQPGPSGPPGPAGMIGPAGPPGKDGEPGRPGRNGDRGIPGLPGHKGHPGMPGMPGMKGARGFDGKDGAKGDSGAPGPKGEAGQPGANGSPGQPGPGGPTGERGRPGNPGGPGAHG... | null | null | extracellular matrix organization [GO:0030198] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872] | PF01410;PF01391;PF00093; | 2.60.120.1000;2.10.70.10; | Fibrillar collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. | Gallus gallus (Chicken) |
P12107 | COBA1_HUMAN | MEPWSSRWKTKRWLWDFTVTTLALTFLFQAREVRGAAPVDVLKALDFHNSPEGISKTTGFCTNRKNSKGSDTAYRVSKQAQLSAPTKQLFPGGTFPEDFSILFTVKPKKGIQSFLLSIYNEHGIQQIGVEVGRSPVFLFEDHTGKPAPEDYPLFRTVNIADGKWHRVAISVEKKTVTMIVDCKKKTTKPLDRSERAIVDTNGITVFGTRILDEEVFEGDIQQFLITGDPKAAYDYCEHYSPDCDSSAPKAAQAQEPQIDEYAPEDIIEYDYEYGEAEYKEAESVTEGPTVTEETIAQTEANIVDDFQEYNYGTMESYQTE... | null | null | cartilage condensation [GO:0001502]; chondrocyte development [GO:0002063]; collagen fibril organization [GO:0030199]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; embryonic skeletal system morphogenesis [GO:0048704]; endodermal cell differentiation [GO:0035987]; extracellular m... | collagen type XI trimer [GO:0005592]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | extracellular matrix binding [GO:0050840]; extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; heparan sulfate binding [GO:1904399]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; protein-macromolecule adaptor act... | PF01410;PF01391;PF02210; | 2.60.120.1000;2.60.120.200; | Fibrillar collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: N-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. | Homo sapiens (Human) |
P12108 | CO9A2_CHICK | MAHRSPALCLLLLHAACLCLAQLRGPPGEPGPRGPPGPPGVPGADGIDGDKGSPGAPGSPGAKGEPGAPGPDGPPGKPGLDGLTGAKGSRGPWGGQGLKGQPGLPGPPGLPGPSLPGPPGLPGQVGLPGEIGVPGPKGDPGPDGPRGPPGPPGKPGPPGHIQGVEGSADFLCPTNCPPGPKGPQGLQGLKGHRGRPGALGEPGQQGKQGPKGDVGVSGEQGVPGPPGPQGQRGYPGMAGPKGETGPAGYKGMVGTIGAAGRPGREGPKGPPGDPGEKGELGGRGIRGPQGDIGPKGDMGLPGIDGKDGTPGIPGVKGTAG... | null | null | extracellular matrix organization [GO:0030198] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01391; | null | Fibril-associated collagens with interrupted helices (FACIT) family | PTM: Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links.; PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:3123475, ECO:0000269|PubMed:3335523, ECO:0000269|PubMed:3473493}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Structural component of hyaline cartilage and vitreous of the eye. | Gallus gallus (Chicken) |
P12109 | CO6A1_HUMAN | MRAARALLPLLLQACWTAAQDEPETPRAVAFQDCPVDLFFVLDTSESVALRLKPYGALVDKVKSFTKRFIDNLRDRYYRCDRNLVWNAGALHYSDEVEIIQGLTRMPGGRDALKSSVDAVKYFGKGTYTDCAIKKGLEQLLVGGSHLKENKYLIVVTDGHPLEGYKEPCGGLEDAVNEAKHLGVKVFSVAITPDHLEPRLSIIATDHTYRRNFTAADWGQSRDAEEAISQTIDTIVDMIKNNVEQVCCSFECQPARGPPGLRGDPGFEGERGKPGLPGEKGEAGDPGRPGDLGPVGYQGMKGEKGSRGEKGSRGPKGYKG... | null | null | 2-oxoglutarate metabolic process [GO:0006103]; adipose tissue development [GO:0060612]; apoptotic nuclear changes [GO:0030262]; autophagy [GO:0006914]; basement membrane organization [GO:0071711]; bone development [GO:0060348]; bone mineralization [GO:0030282]; canonical Wnt signaling pathway [GO:0060070]; cartilage de... | basement membrane [GO:0005604]; collagen type VI trimer [GO:0005589]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intracellular vesicle [GO:0097708]; lysosomal membrane [GO:0005765]; membrane [GO:... | collagen binding [GO:0005518]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; platelet-derived growth factor binding [GO:0048407] | PF01391;PF00092; | 3.40.50.410; | Type VI collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Collagen VI acts as a cell-binding protein. | Homo sapiens (Human) |
P12110 | CO6A2_HUMAN | MLQGTCSVLLLWGILGAIQAQQQEVISPDTTERNNNCPEKTDCPIHVYFVLDTSESVTMQSPTDILLFHMKQFVPQFISQLQNEFYLDQVALSWRYGGLHFSDQVEVFSPPGSDRASFIKNLQGISSFRRGTFTDCALANMTEQIRQDRSKGTVHFAVVITDGHVTGSPCGGIKLQAERAREEGIRLFAVAPNQNLKEQGLRDIASTPHELYRNDYATMLPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPSGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKGVPGFKGEKGEFGADGRKGA... | null | null | cell adhesion [GO:0007155]; neuron apoptotic process [GO:0051402]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; response to glucose [GO:0009749]; response to UV [GO:0009411] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; protein-containing complex [GO:0032991]; sarcolemma ... | collagen binding [GO:0005518]; extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01391;PF00092; | 1.20.5.320;3.40.50.410; | Type VI collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:8305732}. Membrane {ECO:0000269|PubMed:8305732}; Peripheral membrane protein {ECO:0000269|PubMed:8305732}. Note=Recruited on membranes by CSPG4. | null | null | null | null | null | FUNCTION: Collagen VI acts as a cell-binding protein. | Homo sapiens (Human) |
P12111 | CO6A3_HUMAN | MRKHRHLPLVAVFCLFLSGFPTTHAQQQQADVKNGAAADIIFLVDSSWTIGEEHFQLVREFLYDVVKSLAVGENDFHFALVQFNGNPHTEFLLNTYRTKQEVLSHISNMSYIGGTNQTGKGLEYIMQSHLTKAAGSRAGDGVPQVIVVLTDGHSKDGLALPSAELKSADVNVFAIGVEDADEGALKEIASEPLNMHMFNLENFTSLHDIVGNLVSCVHSSVSPERAGDTETLKDITAQDSADIIFLIDGSNNTGSVNFAVILDFLVNLLEKLPIGTQQIRVGVVQFSDEPRTMFSLDTYSTKAQVLGAVKALGFAGGELA... | null | null | cell adhesion [GO:0007155]; muscle organ development [GO:0007517]; neuron apoptotic process [GO:0051402]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; response to glucose [GO:0009749]; response to UV [GO:0009411] | collagen type VI trimer [GO:0005589]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; sarcolemm... | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF01391;PF00014;PF00092; | 2.60.40.10;4.10.410.10;3.40.50.410; | Type VI collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:1689238}.; PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Collagen VI acts as a cell-binding protein. | Homo sapiens (Human) |
P12115 | KAD1_CYPCA | MADKIKDAKIVFVVGGPGSGKGTQCEKIVEKYGYTHLSSGDLLRAEVASGSERGKQLQAIMQKGELVPLDTVLDMIKDAMIAKADVSKGYLIDGYPREVKQGEEFEKKIGAPALLLYIDAKAETMVQRLMKRGQTSGRSDDNEETIKKRLDLYYKATEPVIAYYETRGIVRKINSELPVDEVFAIVVKAIDELK | 2.7.4.3; 2.7.4.6 | null | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550] | PF00406; | 3.40.50.300; | Adenylate kinase family, AK1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03171}; CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:... | null | null | null | null | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. | Cyprinus carpio (Common carp) |
P12154 | PSAA_CHLRE | MTISTPEREAKKVKIAVDRNPVETSFEKWAKPGHFSRTLSKGPNTTTWIWNLHADAHDFDSHTSDLEEISRKVFSAHFGQLGIIFIWLSGMYFHGARFSNYEAWLSDPTHIKPSAQVVWPIVGQEILNGDVGGGFQGIQITSGFFQLWRASGITSELQLYTTAIGGLVMAAAMFFAGWFHYHKAAPKLEWFQNVESMLNHHLGGLLGLGSLAWAGHQIHVSLPVNKLLDAGVDPKEIPLPHDLLLNRAIMADLYPSFAKGIAPFFTLNWSEYSDFLTFKGGLNPVTGGLWLSDTAHHHVAIAVLFLVAGHMYRTNWGIGH... | 1.97.1.12 | COFACTOR: Note=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center. {ECO:0000250}; | photosynthesis [GO:0015979] | chloroplast thylakoid membrane [GO:0009535]; photosystem I [GO:0009522] | 4 iron, 4 sulfur cluster binding [GO:0051539]; chlorophyll binding [GO:0016168]; electron transfer activity [GO:0009055]; magnesium ion binding [GO:0000287]; oxidoreductase activity [GO:0016491] | PF00223; | 1.20.1130.10; | PsaA/PsaB family | null | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036, ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChE... | null | null | null | null | FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair ... | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
P12226 | FGF2_XENLA | MAAGSITTLPTESEDGGNTPFSPGSFKDPKRLYCKNGGFFLRINSDGRVDGSRDKSDSHIKLQLQAVERGVVSIKGITANRYLAMKEDGRLTSLRCITDECFFFERLEANNYNTYRSRKYSSWYVALKRTGQYKNGSSTGPGQKAILFLPMSAKS | null | null | angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cell differentiation in hindbrain [GO:0021533]; fibroblast growth factor receptor signaling pathway [GO:0008543]; lung development [GO:0030324]; mesoderm development [GO:0007498]; nervous system development [GO:0007399]; neural plate anterior/posterior... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; integrin binding [GO:0005178] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09038}. Nucleus {ECO:0000250|UniProtKB:P09038}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (By similarity). Binding of exogenous F... | null | null | null | null | null | FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Also acts as an integrin ligand which is required for FGF2 signaling (By similarity). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration (By similarity). Functions as a potent mi... | Xenopus laevis (African clawed frog) |
P12234 | S25A3_BOVIN | MYSSVVHLARANPFNAPHLQLVHDGLAGPRSDPAGPPGPPRRSRNLAAAAVEEQYSCDYGSGRFFILCGLGGIISCGTTHTALVPLDLVKCRMQVDPQKYKSIFNGFSVTLKEDGFRGLAKGWAPTFIGYSLQGLCKFGFYEVFKVLYSNMLGEENAYLWRTSLYLAASASAEFFADIALAPMEAAKVRIQTQPGYANTLRDAAPKMYKEEGLKAFYKGVAPLWMRQIPYTMMKFACFERTVEALYKFVVPKPRSECSKPEQLVVTFVAGYIAGVFCAIVSHPADSVVSVLNKEKGSSASEVLKRLGFRGVWKGLFARII... | null | null | mitochondrial phosphate ion transmembrane transport [GO:1990547]; phosphate ion transmembrane transport [GO:0035435] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | inorganic phosphate transmembrane transporter activity [GO:0005315]; phosphate:proton symporter activity [GO:0015317]; symporter activity [GO:0015293] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:2036364}; Multi-pass membrane protein {ECO:0000269|PubMed:2036364}. | CATALYTIC ACTIVITY: [Isoform A]: Reaction=H(+)(in) + phosphate(in) = H(+)(out) + phosphate(out); Xref=Rhea:RHEA:29939, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:9712911}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29941; Evidence={ECO:0000305|PubMed:9712911}; CATALYTIC ACTIVITY: [Isof... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.1 mM for phosphate {ECO:0000269|PubMed:9712911}; Kinetic parameters: KM=7 mM for phosphate {ECO:0000269|PubMed:9712911}; | null | null | null | FUNCTION: Inorganic ion transporter that transports phosphate or copper ions across the mitochondrial inner membrane into the matrix compartment (By similarity) (PubMed:9712911). Mediates proton-coupled symport of phosphate ions necessary for mitochondrial oxidative phosphorylation of ADP to ATP (PubMed:9712911). Trans... | Bos taurus (Bovine) |
P12235 | ADT1_HUMAN | MGDHAWSFLKDFLAGGVAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQLFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFHGLGDCIIKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIFVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGAKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV | null | null | adaptive thermogenesis [GO:1990845]; ADP transport [GO:0015866]; apoptotic mitochondrial changes [GO:0008637]; generation of precursor metabolites and energy [GO:0006091]; mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; mitochondrial genome maintenance [GO... | membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial permeability transition pore complex [GO:0005757]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | adenine transmembrane transporter activity [GO:0015207]; ATP:ADP antiporter activity [GO:0005471]; oxidative phosphorylation uncoupler activity [GO:0017077]; proton transmembrane transporter activity [GO:0015078] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: Under cell death induction, transglutaminated by TGM2. Transglutamination leads to formation of covalent cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming polymers. {ECO:0000250|UniProtKB:P48962}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21586654}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:27641616}; Multi-pass membrane protein {ECO:0000255}. Note=The complex formed with ARL2BP, ARL2 and SLC25A4/ANT1 is expressed in mitochondria (By similarity). May loc... | CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:21586654}; CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P48962}; | null | null | null | null | FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:21586654, PubMed:27693233). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with ... | Homo sapiens (Human) |
P12236 | ADT3_HUMAN | MTEQAISFAKDFLAGGIAAAISKTAVAPIERVKLLLQVQHASKQIAADKQYKGIVDCIVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKHTQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKSGTEREFRGLGDCLVKITKSDGIRGLYQGFSVSVQGIIIYRAAYFGVYDTAKGMLPDPKNTHIVVSWMIAQTVTAVAGVVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIFRDEGGKAFFKGAWSNVLRGMGGAFVLVLYDELKKVI | null | null | apoptotic process [GO:0006915]; mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029] | membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; TIM23 mitochondrial import inner membrane translocase complex [GO:0005744] | ATP:ADP antiporter activity [GO:0005471] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: Trimethylated by ANTKMT at Lys-52. {ECO:0000269|PubMed:31213526}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P02722}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:27641616}; Multi-pass membrane protein {ECO:0000255}. Note=The complex formed with ARL2BP, ARL2 and SLC25A6/ANT3 is expressed in mitochondria (By similarity). May lo... | CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P48962}; CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:P48962}; | null | null | null | null | FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-... | Homo sapiens (Human) |
P12238 | PSBE_THEVL | MAGTTGERPFSDIITSVRYWVIHSITIPALFIAGWLFVSTGLAYDVFGTPRPDSYYAQEQRSIPLVTDRFEAKQQVETFLEQLK | null | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Note=With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids. {EC... | photosynthetic electron transport chain [GO:0009767] | photosystem II reaction center [GO:0009539]; plasma membrane-derived thylakoid membrane [GO:0031676] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00283;PF00284; | 1.20.5.860; | PsbE/PsbF family | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00642, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803... | null | null | null | null | null | FUNCTION: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core an... | Thermostichus vulcanus (Synechococcus vulcanus) |
P12239 | PSBF_THEVL | MTSNTPNQEPVSYPIFTVRWVAVHTLAVPTIFFLGAIAAMQFIQR | null | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_00643}; Note=With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260... | photosynthetic electron transport chain [GO:0009767] | photosystem II reaction center [GO:0009539]; plasma membrane-derived thylakoid membrane [GO:0031676] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00283; | null | PsbE/PsbF family | null | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803, ECO:0000269|PubMed:21499260, ECO:0000269|PubMed:23426624}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00643, ECO:0000269|PubMed:12518057, ECO:0000269|PubMed:19433803... | null | null | null | null | null | FUNCTION: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core an... | Thermostichus vulcanus (Synechococcus vulcanus) |
P12242 | UCP1_MOUSE | MVNPTTSEVQPTMGVKIFSAGVSACLADIITFPLDTAKVRLQIQGEGQASSTIRYKGVLGTITTLAKTEGLPKLYSGLPAGIQRQISFASLRIGLYDSVQEYFSSGRETPASLGNKISAGLMTGGVAVFIGQPTEVVKVRMQAQSHLHGIKPRYTGTYNAYRVIATTESLSTLWKGTTPNLMRNVIINCTELVTYDLMKGALVNNKILADDVPCHLLSALVAGFCTTLLASPVDVVKTRFINSLPGQYPSVPSCAMSMYTKEGPTAFFKGFVASFLRLGSWNVIMFVCFEQLKKELMKSRQTVDCTT | null | null | adaptive thermogenesis [GO:1990845]; brown fat cell differentiation [GO:0050873]; cellular response to cold [GO:0070417]; cellular response to dehydroepiandrosterone [GO:1903495]; cellular response to fatty acid [GO:0071398]; cellular response to hormone stimulus [GO:0032870]; cellular response to reactive oxygen speci... | mitochondrial envelope [GO:0005740]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | cardiolipin binding [GO:1901612]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; long-chain fatty acid binding [GO:0036041]; oxidative phosphorylation uncoupler activity [GO:0017077]; proton transmembrane transporter activity [GO:0015078]; purine ribonucleotide binding [GO:0032555]; transmembrane transporter activ... | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | PTM: Sulfenylation at Cys-254 is increased upon cold exposure. It increases the sensitivity of UCP1 thermogenic function to the activation by noradrenaline probably through structural effects. {ECO:0000269|PubMed:27027295}.; PTM: May undergo ubiquitin-mediated proteasomal degradation. {ECO:0000250|UniProtKB:P04633}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23063128}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04633}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:23063128}; | null | null | null | null | FUNCTION: Mitochondrial transporter that functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport... | Mus musculus (Mouse) |
P12246 | SAMP_MOUSE | MDKLLLWMFVFTSLLSEAFCQTDLKRKVFVFPRESETDHVKLIPHLEKPLQNFTLCFRTYSDLSRSQSLFSYSVKGRDNELLIYKEKVGEYSLYIGQSKVTVRGMEEYLSPVHLCTTWESSSGIVEFWVNGKPWVKKSLQREYTVKAPPSIVLGQEQDNYGGGFQRSQSFVGEFSDLYMWDYVLTPQDILFVYRDSPVNPNILNWQALNYEINGYVVIRPRVWD | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 2 calcium ions per subunit. {ECO:0000250}; | innate immune response [GO:0045087]; negative regulation by host of viral exo-alpha-sialidase activity [GO:0044869]; negative regulation by host of viral glycoprotein metabolic process [GO:0044871]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of viral entry into host cell [GO:00465... | extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; complement component C1q complex binding [GO:0001849]; identical protein binding [GO:0042802]; virion binding [GO:0046790] | PF00354; | 2.60.120.200; | Pentraxin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | null | Mus musculus (Mouse) |
P12252 | PDE4B_DROME | MSQESNGGPAAGGGAAAAPPPPPQYIITTPSEVDPDEVRSMADLELGSPEKQVQVQSQKFSSTSSTTKVATHSFSMSSSAGTTGQQSKQDSAQQIQQLQQLQQLQQLQQQQQQQQSQRIISSSTRSQSLQSSTIVGEATTITSGAAQILSASAAASLAQQLKAQSSTSIITSSEQRTSTSTSSSSSTRYIASGSSNLAGGNSNSASSASSKTRFQSFLQQPEGAHGFLTAHQKHVRQFVRSTSAHSEAAAGVAGARAEKCIRSASTQIDDASVAGVVESAGNLTDSSATGGSMQLSMSKLGLQQSSSILISKSAETIEMK... | 3.1.4.53 | COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:Q07343}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250|UniProtKB:Q07343}; | anesthesia-resistant memory [GO:0007615]; associative learning [GO:0008306]; axon extension [GO:0048675]; cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; chemical synaptic transmission [GO:0007268]; circadian rhythm [GO:0007623]; conditioned taste aversion [GO:0001661]; courtship behavior [GO... | cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; synapse [GO:0045202] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872] | PF18100;PF00233; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE4 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000269|PubMed:1660926}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278; Evidence={ECO:0000305|PubMed:1660926}; | null | PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. {ECO:0000250|UniProtKB:Q07343}. | null | null | FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (By similarity). Vital for female fertility. Required for learning/memory. {ECO:0000250, ECO:0000269|PubMed:1660926}. | Drosophila melanogaster (Fruit fly) |
P12256 | PAC_LYSSH | MLGCSSLSIRTTDDKSLFARTMDFTMEPDSKVIIVPRNYGIRLLEKENVVINNSYAFVGMGSTDITSPVLYDGVNEKGLMGAMLYYATFATYADEPKKGTTGINPVYVISQVLGNCVTVDDVIEKLTSYTLLNEANIILGFAPPLHYTFTDASGESIVIEPDKTGITIHRKTIGVMTNSPGYEWHQTNLRAYIGVTPNPPQDIMMGDLDLTPFGQGAGGLGLPGDFTPSARFLRVAYWKKYTEKAKNETEGVTNLFHILSSVNIPKGVVLTNEGKTDYTIYTSAMCAQSKNYYFKLYDNSRISAVSLMAENLNSQDLITF... | 3.5.1.11 | null | response to antibiotic [GO:0046677] | null | penicillin amidase activity [GO:0008953] | PF02275; | null | Peptidase C59 family | PTM: Expressed as an inactive precursor that is cleaved autocatalytically at Gly-3/Cys-4 to generate an active enzyme (PubMed:10331865, PubMed:16508111). Processing exposes a catalytic N-terminal nucleophile residue with a free alpha amino group (PubMed:10331865). {ECO:0000269|PubMed:10331865, ECO:0000269|PubMed:165081... | null | CATALYTIC ACTIVITY: Reaction=a penicillin + H2O = 6-aminopenicillanate + a carboxylate; Xref=Rhea:RHEA:18693, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:51356, ChEBI:CHEBI:57869; EC=3.5.1.11; Evidence={ECO:0000269|PubMed:30243389, ECO:0000269|PubMed:9009066}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21.95 mM for penicillin V {ECO:0000269|PubMed:30243389}; Vmax=10.22 umol/min/mg enzyme {ECO:0000269|PubMed:30243389}; Note=kcat is 6.38 sec(-1). {ECO:0000269|PubMed:30243389}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 (PubMed:30243389). Is very stable at pH 6.0-7.0 (PubMed:30243389). {ECO:0000269|PubMed:30243389}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius (PubMed:30243389). Is very stable at 30-40 degrees Celsius (PubMed:30243389). {ECO:0000269|PubMed:30243389}; | FUNCTION: Catalyzes the hydrolysis of penicillin V to 6-aminopenicillanate (6-APA) (PubMed:30243389, PubMed:3026906, PubMed:9009066). Exhibits high specificity for penicillin V (PubMed:9009066). Penicillin G and other related compounds are hydrolyzed at less than 10% of the rate of penicillin V (PubMed:9009066). Among ... | Lysinibacillus sphaericus (Bacillus sphaericus) |
P12259 | FA5_HUMAN | MFPGCPRLWVLVVLGTSWVGWGSQGTEAAQLRQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLLICKKGTLTEGGTQKTFDKQIVLLFAVFDESKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGM... | null | null | blood circulation [GO:0008015]; blood coagulation [GO:0007596]; response to vitamin K [GO:0032571] | COPII-coated ER to Golgi transport vesicle [GO:0030134]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; membrane [GO:0016020]; plasma membrane [... | copper ion binding [GO:0005507]; signaling receptor activity [GO:0038023] | PF07732;PF00754; | 2.60.40.420;2.60.120.260; | Multicopper oxidase family | PTM: Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus).; PTM: Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity. {ECO:0000269|PubMed:2168225, ECO:0000269|P... | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin. | Homo sapiens (Human) |
P12265 | BGLR_MOUSE | MSLKWSACWVALGQLLCSCALALKGGMLFPKESPSRELKALDGLWHFRADLSNNRLQGFEQQWYRQPLRESGPVLDMPVPSSFNDITQEAALRDFIGWVWYEREAILPRRWTQDTDMRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADISKLVQSGPLTTCRITIAINNTLTPHTLPPGTIVYKTDTSMYPKGYFVQDTSFDFFNYAGLHRSVVLYTTPTTYIDDITVITNVEQDIGLVTYWISVQGSEHFQLEVQLLDEGGKVVAHGTGNQGQLQVPSANLWWPYLMHEHPAYMYSLEVKVTTTESVTDYYTLPI... | 3.2.1.31 | null | carbohydrate metabolic process [GO:0005975]; chondroitin sulfate catabolic process [GO:0030207]; glucuronoside catabolic process [GO:0019391]; heparan sulfate proteoglycan catabolic process [GO:0030200]; hyaluronan catabolic process [GO:0030214] | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764] | beta-glucuronidase activity [GO:0004566]; carbohydrate binding [GO:0030246]; hydrolase activity [GO:0016787]; protein domain specific binding [GO:0019904]; signaling receptor binding [GO:0005102] | PF00703;PF02836;PF02837; | 2.60.120.260;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 2 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:2394691}. Endoplasmic reticulum {ECO:0000269|PubMed:2394691}. Note=A small proportion is found in the endoplasmic reticulum. | CATALYTIC ACTIVITY: Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31; | null | null | null | null | FUNCTION: Plays an important role in the degradation of dermatan and keratan sulfates. | Mus musculus (Mouse) |
P12268 | IMDH2_HUMAN | MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDA... | 1.1.1.205 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; | 'de novo' XMP biosynthetic process [GO:0097294]; cellular response to interleukin-4 [GO:0071353]; circadian rhythm [GO:0007623]; GMP biosynthetic process [GO:0006177]; GTP biosynthetic process [GO:0006183]; lymphocyte proliferation [GO:0046651] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleus [GO:0005634]; peroxisomal membrane [GO:0005778]; secretory granule lumen [GO:0034774] | DNA binding [GO:0003677]; IMP dehydrogenase activity [GO:0003938]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723] | PF00571;PF00478; | 3.20.20.70; | IMPDH/GMPR family | PTM: Ubiquitinated leading to its degradation by the proteasome. {ECO:0000269|PubMed:30293565}.; PTM: The N-terminus is blocked.; PTM: Acetylated by CLOCK in a circadian manner (PubMed:28985504). {ECO:0000269|PubMed:28985504}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14766016}. Nucleus {ECO:0000269|PubMed:14766016}. Cytoplasm, cytosol {ECO:0000269|PubMed:31337707}. Note=Can form fiber-like subcellular structures termed 'cytoophidia' in response to intracellular guanine-nucleotide depletion. {ECO:0000269|PubMed:24477477, ECO:000026... | CATALYTIC ACTIVITY: Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000269|PubMed:7763314, ECO:0000269|PubMed:7903306}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.3 uM for Inosine 5'-phosphate {ECO:0000269|PubMed:7763314, ECO:0000269|PubMed:7903306}; KM=32 uM for NAD(+) {ECO:0000269|PubMed:7763314, ECO:0000269|PubMed:7903306}; | PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000269|PubMed:7763314, ECO:0000269|PubMed:7903306}. | null | null | FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (PubMed:7763314, PubMed:7903306). Could also have a single... | Homo sapiens (Human) |
P12269 | IMDH2_CRIGR | MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDRFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNENDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLALAGVDVVVLDSSQGNSIFQINMIKYMKEKYPNLQVIGGNVVTAAQAKNLIDAGVDA... | 1.1.1.205 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; | 'de novo' XMP biosynthetic process [GO:0097294]; cellular response to interleukin-4 [GO:0071353]; circadian rhythm [GO:0007623]; GMP biosynthetic process [GO:0006177]; GTP biosynthetic process [GO:0006183]; lymphocyte proliferation [GO:0046651] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | IMP dehydrogenase activity [GO:0003938]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166] | PF00571;PF00478; | 3.20.20.70; | IMPDH/GMPR family | PTM: Acetylated by CLOCK in a circadian manner. {ECO:0000250|UniProtKB:P12268}.; PTM: Ubiquitinated leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P12268}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P12268}. Nucleus {ECO:0000250|UniProtKB:P12268}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P12268}. Note=Can form fiber-like subcellular structures termed 'cytoophidia' in response to intracellular guanine-nucleotide depletion. {ECO:0000250|UniProtKB:P12268}. | CATALYTIC ACTIVITY: Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000250|UniProtKB:P12268}; | null | PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. {ECO:0000250|UniProtKB:P12268}. | null | null | FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding ac... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P12270 | TPR_HUMAN | MAAVLQQVLERTELNKLPKSVQNKLEKFLADQQSEIDGLKGRHEKFKVESEQQYFEIEKRLSHSQERLVNETRECQSLRLELEKLNNQLKALTEKNKELEIAQDRNIAIQSQFTRTKEELEAEKRDLIRTNERLSQELEYLTEDVKRLNEKLKESNTTKGELQLKLDELQASDVSVKYREKRLEQEKELLHSQNTWLNTELKTKTDELLALGREKGNEILELKCNLENKKEEVSRLEEQMNGLKTSNEHLQKHVEDLLTKLKEAKEQQASMEEKFHNELNAHIKLSNLYKSAADDSEAKSNELTRAVEELHKLLKEAGEA... | null | null | cell division [GO:0051301]; cellular response to heat [GO:0034605]; cellular response to interferon-alpha [GO:0035457]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mRNA export from nucleus [GO:0006406]; mRNA export from nucleus in response to heat stress [GO:0031990]; negative regulation of RNA export f... | cytoplasm [GO:0005737]; cytoplasmic dynein complex [GO:0005868]; kinetochore [GO:0000776]; mitotic spindle [GO:0072686]; nuclear envelope [GO:0005635]; nuclear inclusion body [GO:0042405]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear basket [GO:0044615];... | chromatin binding [GO:0003682]; dynein complex binding [GO:0070840]; heat shock protein binding [GO:0031072]; mitogen-activated protein kinase binding [GO:0051019]; mRNA binding [GO:0003729]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; structural constituent of nuclear pore [GO:0017056]; t... | PF07926; | 1.10.287.1490; | TPR family | PTM: Phosphorylated. Phosphorylation occurs on serine and threonine residues (comprised in the C-terminal region) by MAPK1/ERK2 and stabilizes the interaction between these two proteins. {ECO:0000269|PubMed:18794356}.; PTM: Proteolytically degraded after poliovirus (PV) infection; degradation is restricted to its unfol... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12802065}. Nucleus membrane {ECO:0000269|PubMed:11514627, ECO:0000269|PubMed:11952838, ECO:0000269|PubMed:18794356, ECO:0000269|PubMed:9024684, ECO:0000269|PubMed:9828100, ECO:0000269|PubMed:9864356}; Peripheral membrane protein {ECO:0000269|PubMed:11514627, ECO:0000269... | null | null | null | null | null | FUNCTION: Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs, plays a role in the establishment of nuclear-peripheral ch... | Homo sapiens (Human) |
P12271 | RLBP1_HUMAN | MSEGVGTFRMVPEEEQELRAQLEQLTTKDHGPVFGPCSQLPRHTLQKAKDELNEREETREEAVRELQEMVQAQAASGEELAVAVAERVQEKDSGFFLRFIRARKFNVGRAYELLRGYVNFRLQYPELFDSLSPEAVRCTIEAGYPGVLSSRDKYGRVVMLFNIENWQSQEITFDEILQAYCFILEKLLENEETQINGFCIIENFKGFTMQQAASLRTSDLRKMVDMLQDSFPARFKAIHFIHQPWYFTTTYNVVKPFLKSKLLERVFVHGDDLSGFYQEIDENILPSDFGGTLPKYDGKAVAEQLFGPQAQAENTAF | null | null | response to stimulus [GO:0050896]; visual perception [GO:0007601]; vitamin A metabolic process [GO:0006776] | cell body [GO:0044297]; centrosome [GO:0005813]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654] | 11-cis retinal binding [GO:0005502]; phosphatidylinositol bisphosphate binding [GO:1902936]; retinol binding [GO:0019841] | PF00650;PF03765; | 3.40.525.10;1.10.8.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metaboli... | Homo sapiens (Human) |
P12272 | PTHR_HUMAN | MQRRLVQQWSVAVFLLSYAVPSCGRSVEGLSRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPSPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRKEQEKKKRRTRSAWLDSGVTGSGLEGDHLSDTSTTSLELDSRRH | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; cAMP metabolic process [GO:0046058]; cell-cell signaling [GO:0007267]; epidermis development [GO:0008544]; female pregnancy [GO:0007565]; negative regulation of cell population proliferation [GO:000... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654] | hormone activity [GO:0005179]; peptide hormone receptor binding [GO:0051428] | PF01279; | null | Parathyroid hormone family | PTM: There are 3 principal secretory forms, called PTHrP[1-36], PTHrP[38-94], and osteostatin (PTHrP[107-139]) arising from endoproteolytic cleavage of the initial translation product. Each of these secretory forms is believed to have one or more of its own receptors that mediates the normal paracrine, autocrine and en... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted. | null | null | null | null | null | FUNCTION: Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport. Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth.... | Homo sapiens (Human) |
P12273 | PIP_HUMAN | MRLLQLLFRASPATLLLVLCLQLGANKAQDNTRKIIIKNFDIPKSVRPNDEVTAVLAVQTELKECMVVKTYLISSIPLQGAFNYKYTACLCDDNPKTFYWDFYTNRTVQIAAVVDVIRELGICPDDAAVIPIKNNRFYTIEILKVE | null | null | detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; negative regulation of T cell apoptotic process [GO:0070233]; positive regulation of gene expression [GO:0010628]; proteolysis [GO:0006508]; regulation of immune system process [GO:0002682] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634] | actin binding [GO:0003779]; aspartic-type endopeptidase activity [GO:0004190]; identical protein binding [GO:0042802]; IgG binding [GO:0019864] | PF05326; | 2.60.40.10; | PIP family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | null | Homo sapiens (Human) |
P12276 | FAS_CHICK | MEDVVIAGIAGKLPESENLQEFWENLLNGVDMVTEDDRRWKPGIYGLPKRNGKLKDIKKFDASFFGVHPKQAHTMDPQLRLLLEVSYEAILDGGINPTALRGTDTGVWVGASGSEALEALSQDPEELLGYSMTGCQRAMLANRISYFYDFTGPSLTIDTACSSSLMALENAYKAIRHGQCSAALVGGVNILLKPNTSVQFMKLGMLSPDGACKAFDVSGNGYCRSEAVVVVLLTKKSMAKRVYATIVNAGSNTDGFKEQGVTFPSGEMQQQLVGSLYRECGIKPGDVEYVEAHGTGTKVGDPQEVNGIVNVFCQCEREPL... | 1.1.1.100; 1.3.1.39; 2.3.1.38; 2.3.1.39; 2.3.1.41; 2.3.1.85; 3.1.2.14; 4.2.1.59 | null | fatty acid biosynthetic process [GO:0006633]; lactate metabolic process [GO:0006089]; positive regulation of appetite [GO:0032100] | cytoplasm [GO:0005737] | (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity [GO:0047450]; (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity [GO:0008693]; (3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity [GO:0008659]; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity [GO:0047451... | PF00698;PF00107;PF21149;PF16197;PF00109;PF02801;PF08659;PF21089;PF00550;PF00975; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150; | null | PTM: S-nitrosylation of Fatty acid synthase at cysteine residues Cys-1475 or Cys-2093 is important for the enzyme dimerization. In adipocytes, S-nitrosylation of Fatty acid synthase occurs under physiological conditions and gradually increases during adipogenesis. {ECO:0000250|UniProtKB:P49327}. | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:3182791, ECO:0000269|PubMed:6361031, ECO:0000269|PubMed:6654913, ECO:0000269|PubMed:6654914}. | null | null | FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-ph... | Gallus gallus (Chicken) |
P12277 | KCRB_HUMAN | MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTGVDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFSEVLKRLRLQKR... | 2.7.3.2 | null | futile creatine cycle [GO:0140651]; phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310]; substantia nigra development [GO:0021762] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; creatine kinase activity [GO:0004111]; ubiquitin protein ligase binding [GO:0031625] | PF00217;PF02807; | 1.10.135.10;3.30.590.10; | ATP:guanido phosphotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q04447}. Mitochondrion {ECO:0000250|UniProtKB:Q04447}. Cell membrane {ECO:0000269|PubMed:18566107}. Note=Localizes to the mitochondria of thermogenic fat cells via the internal MTS-like signal (iMTS-L) region. {ECO:0000250|UniProtKB:Q04447}. | CATALYTIC ACTIVITY: Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10029, ECO:0000269|PubMed:8186255}; PhysiologicalDirection=left-to-righ... | null | null | null | null | FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:8186255). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (Probabl... | Homo sapiens (Human) |
P12281 | MOEA_ECOLI | MEFTTGLMSLDTALNEMLSRVTPLTAQETLPLVQCFGRILASDVVSPLDVPGFDNSAMDGYAVRLADIASGQPLPVAGKSFAGQPYHGEWPAGTCIRIMTGAPVPEGCEAVVMQEQTEQMDNGVRFTAEVRSGQNIRRRGEDISAGAVVFPAGTRLTTAELPVIASLGIAEVPVIRKVRVALFSTGDELQLPGQPLGDGQIYDTNRLAVHLMLEQLGCEVINLGIIRDDPHALRAAFIEADSQADVVISSGGVSVGEADYTKTILEELGEIAFWKLAIKPGKPFAFGKLSNSWFCGLPGNPVSATLTFYQLVQPLLAKLS... | 2.10.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11428898}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:11428898}; | Mo-molybdopterin cofactor biosynthetic process [GO:0006777] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin molybdotransferase activity [GO:0061599]; protein homodimerization activity [GO:0042803] | PF00994;PF03454;PF03453; | 3.40.980.10;2.40.340.10;3.90.105.10;2.170.190.11; | MoeA family | null | null | CATALYTIC ACTIVITY: Reaction=adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin; Xref=Rhea:RHEA:35047, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:36264, ChEBI:CHEBI:62727, ChEBI:CHEBI:71302, ChEBI:CHEBI:456215; EC=2.10.1.1; Evidence={ECO:0000269|PubMed:15632135}; | null | PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. | null | null | FUNCTION: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. {ECO:0000269|PubMed:15632135}. | Escherichia coli (strain K12) |
P12282 | MOEB_ECOLI | MAELSDQEMLRYNRQIILRGFDFDGQEALKDSRVLIVGLGGLGCAASQYLASAGVGNLTLLDFDTVSLSNLQRQTLHSDATVGQPKVESARDALTRINPHIAITPVNALLDDAELAALIAEHDLVLDCTDNVAVRNQLNAGCFAAKVPLVSGAAIRMEGQITVFTYQDGEPCYRCLSRLFGENALTCVEAGVMAPLIGVIGSLQAMEAIKMLAGYGKPASGKIVMYDAMTCQFREMKLMRNPGCEVCGQ | 2.7.7.80 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11463785}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11463785}; | Mo-molybdopterin cofactor biosynthetic process [GO:0006777] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; molybdopterin cofactor (Moco) biosynthesis adenylyltransferase complex [GO:1990133] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; nucleotidyltransferase activity [GO:0016779]; protein homodimerization activity [GO:0042803]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; ubiquitin... | PF00899; | 3.40.50.720; | HesA/MoeB/ThiF family | null | null | CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ... | null | PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. | null | null | FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD. {ECO:0000269|PubMed:11290749, ECO:0000269|PubMed:11463785}. | Escherichia coli (strain K12) |
P12293 | DHM1_PARDE | MNRNTPKARGASSLAMAVAMGLAVLTTAPATANDQLVELAKDPANWVMTGRDYNAQNYSEMTDINKENVKQLRPAWSFSTGVLHGHEGTPLVVGDRMFIHTPFPNTTFALDLNEPGKILWQNKPKQNPTARTVACCDVVNRGLAYWPGDDQVKPLIFRTQLDGHIVAMDAETGETRWIMENSDIKVGSTLTIAPYVIKDLVLVGSSGAELGVRGYVTAYDVKSGEMRWRAFATGPDEELLLAEDFNAPNPHYGQKNLGLETWEGDAWKIGGGTNWGWYAYDPEVDLFYYGSGNPAPWNETMRPGDNKWTMAIWGREATTG... | 1.1.2.7 | COFACTOR: Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; Evidence={ECO:0000269|PubMed:14505072}; Note=Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-135-Cys-136 and the indole ring of Trp-275. {ECO:0000269|PubMed:14505072}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:00002... | methanol metabolic process [GO:0015945] | membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288] | alcohol dehydrogenase (cytochrome c(L)) activity [GO:0052933]; calcium ion binding [GO:0005509] | PF13360; | 2.140.10.10; | Bacterial PQQ dehydrogenase family | null | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + 2 Fe(III)-[cytochrome cL] = an aldehyde + 2 Fe(II)-[cytochrome cL] + 2 H(+); Xref=Rhea:RHEA:51004, Rhea:RHEA-COMP:12863, Rhea:RHEA-COMP:12864, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.7; | null | null | null | null | FUNCTION: Catalyzes the oxidation of primary alcohols including methanol. {ECO:0000250}. | Paracoccus denitrificans |
P12294 | ENS2_YEASX | MKKQNLNSILLMYINYIINYFNNIHKNQLKKDWIMEYEYMYKFLMNNMTCFIKWDNNKILLLLDMYYNVLYNYHKQRTPMSNKRLMNSKNIMDYKLLYTYFYILNKMKMEMDNYNNNNNNISLKYNELLKNIMNNLNYKTSNIETNLSNNFYLMDKYLINKYMKYLDMLNMIPNNYMFNNINYKGKLNIKTVLDLNNNEFYDYLSGLIEGDGYIGPGGITITNHANDVLNTIFINKRIKNSILVEKWMDTLKDNPYFVNAFSINIKTNLAKEKIFTNIYNKLYSDYKINQINNHIPYYNYLKINNKLPIKNIMDIKNNYW... | 3.1.21.- | null | mitochondrial DNA metabolic process [GO:0032042]; regulation of DNA recombination [GO:0000018] | endodeoxyribonuclease complex [GO:1905347]; mitochondrion [GO:0005739] | endonuclease activity [GO:0004519] | PF00961; | 3.10.28.10; | LAGLIDADG endonuclease family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Mitochondrion. | null | null | null | null | null | FUNCTION: Catalytic component of endonuclease SceI (Endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. {ECO:0000269|PubMed:10464305, ECO:0000269|PubMed:1988456, ECO:0000269|PubMed:2828049, ECO:0000269|PubMed:7625280}. | Saccharomyces cerevisiae (Baker's yeast) |
P12295 | UNG_ECOLI | MANELTWHDVLAEEKQQPYFLNTLQTVASERQSGVTIYPPQKDVFNAFRFTELGDVKVVILGQDPYHGPGQAHGLAFSVRPGIAIPPSLLNMYKELENTIPGFTRPNHGYLESWARQGVLLLNTVLTVRAGQAHSHASLGWETFTDKVISLINQHREGVVFLLWGSHAQKKGAIIDKQRHHVLKAPHPSPLSAHRGFFGCNHFVLANQWLEQRGETPIDWMPVLPAESE | 3.2.2.27 | null | base-excision repair, AP site formation via deaminated base removal [GO:0097510] | cytoplasm [GO:0005737] | uracil DNA N-glycosylase activity [GO:0004844] | PF03167; | 3.40.470.10; | Uracil-DNA glycosylase (UDG) superfamily, UNG family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27; | null | null | null | null | FUNCTION: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | Escherichia coli (strain K12) |
P12296 | POLG_ENMGO | MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQGNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANATGSDPPKTYGQFSNLLSGAVNAFSNMLPLLADQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGATLRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNRWSKDNLPNGTRTQTNRKGPFAMDHQNFWQWTLYPHQFL... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; positive stranded viral RNA replication [GO:0039690]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF00548;PF00680;PF00073;PF00910;PF08935;PF11475; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protein]: Phosphorylated. {ECO:0000269|PubMed:25331866}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (PubMed:8972564). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000269|PubMed:2156078, ECO:0000269|PubMed:3026048}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000269|PubMed:2156078, ECO:0000269|PubMed:3026048}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:24600002}; CATALYTI... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for protease 3C. {ECO:0000269|PubMed:8972564}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius for protease 3C. {ECO:0000269|PubMed:8972564}; | FUNCTION: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (By similarity). Proteins with NLS signals f... | Mengo encephalomyocarditis virus |
P12299 | GLGL2_WHEAT | MSSMQFSSVLPLEGKACISPVRREGSASERLKVGDSSSIRHERASRRMCNGGRGPAATGAQCVLTSDASPADTLVLRTSFRRNYADPNEVAAVILGGGTGTQLFPLTSTRATPAVPIGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHRTYLGGGINFTDGSVEVLAATQMPGEAAGWFRGTADAVRKFIWVLEDYYKNKSIEHILILSGDQLYRMDYMELVQKHVDDNADITLSCAPVGESRASEYGLVKFDSSGRVVQFSEKPKGDDLEAMKVDTSFLNFAIDDPAKYPYIASMGVYVFKRDVLLNLLKSR... | 2.7.7.27 | null | glycogen biosynthetic process [GO:0005978]; starch biosynthetic process [GO:0019252] | amyloplast [GO:0009501]; chloroplast [GO:0009507] | ATP binding [GO:0005524]; glucose-1-phosphate adenylyltransferase activity [GO:0008878] | PF00483; | 2.160.10.10; | Bacterial/plant glucose-1-phosphate adenylyltransferase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. Note=Found in the chloroplast in leaf. Found in the plastid in the developing endosperm. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498, ChEBI:CHEBI:58601; EC=2.7.7.27; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. | null | null | FUNCTION: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP. | Triticum aestivum (Wheat) |
P12300 | GLGL3_WHEAT | RASPPSESRAPLRAPQRSATRQHQARQGPRRMCNGGRGPPYWTAGVTSAPARQTPLFSGRPSGGLSDPNEVAAVILGGGTGTQLFPLTSTRATPAVPIGGCYRLIDIPMSNCFNSGINKIFVMTQFNSASLNRHIHRTYLGGGINFTDGSVEVLAATQMPGEAAGWFRGTADAWRKIIWVLEDYYKNKSIEHILILSGDQLYRMDYMELVQKHVDDNADITLSCAPVGESRASEYGLVKFDSSGRVVQFSEQPKGDDLEAMKVDTSFLNFAIDDPAKYPYIASMGVYVFKRDVLLNLLKSRYAELHDFGSEILPRALHDH... | 2.7.7.27 | null | glycogen biosynthetic process [GO:0005978]; starch biosynthetic process [GO:0019252] | amyloplast [GO:0009501]; chloroplast [GO:0009507] | ATP binding [GO:0005524]; glucose-1-phosphate adenylyltransferase activity [GO:0008878] | PF00483; | 2.160.10.10; | Bacterial/plant glucose-1-phosphate adenylyltransferase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. Note=Found in the chloroplast in leaf. Found in the plastid in the developing endosperm. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498, ChEBI:CHEBI:58601; EC=2.7.7.27; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. | null | null | FUNCTION: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP. | Triticum aestivum (Wheat) |
P12314 | FCGR1_HUMAN | MWFLTTLLLWVPVDGQVDTTKAVITLQPPWVSVFQEETVTLHCEVLHLPGSSSTQWFLNGTATQTSTPSYRITSASVNDSGEYRCQRGLSGRSDPIQLEIHRGWLLLQVSSRVFTEGEPLALRCHAWKDKLVYNVLYYRNGKAFKFFHWNSNLTILKTNISHNGTYHCSGMGKHRYTSAGISVTVKELFPAPVLNASVTSPLLEGNLVTLSCETKLLLQRPGLQLYFSFYMGSKTLRGRNTSSEYQILTARREDSGLYWCEAATEDGNVLKRSPELELQVLGLQLPTPVWFHVLFYLAVGIMFLVNTVLWVTIRKELKRK... | null | null | antibody-dependent cellular cytotoxicity [GO:0001788]; antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; cell surface receptor signaling pathway [GO:0007166]; defense response to bacterium [GO:0042742]; immune response [GO:0006955]; innate immune response [GO:0045087]; phago... | clathrin-coated endocytic vesicle membrane [GO:0030669]; early endosome membrane [GO:0031901]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | high-affinity IgG receptor activity [GO:0019771]; IgG binding [GO:0019864]; IgG receptor activity [GO:0019770] | PF00047;PF13895;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, FCGR1 family | PTM: Phosphorylated on serine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12756162, ECO:0000269|PubMed:8611682}; Single-pass type I membrane protein {ECO:0000269|PubMed:12756162, ECO:0000269|PubMed:8611682}. Note=Stabilized at the cell membrane through interaction with FCER1G. | null | null | null | null | null | FUNCTION: High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses. Mediates IgG effector functions on monocytes triggering antibody-dependent cellular cytotoxicity (ADCC) of virus-infected cells. {ECO:0000269|PubMed:10397749, ECO:0000269|PubMed:10514529,... | Homo sapiens (Human) |
P12318 | FCG2A_HUMAN | MTMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDDKNIYLTLPPNDHVNSNN | null | null | antibody-dependent cellular cytotoxicity [GO:0001788]; cell surface receptor signaling pathway [GO:0007166]; positive regulation of phagocytosis [GO:0050766]; positive regulation of tumor necrosis factor production [GO:0032760] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667] | IgG binding [GO:0019864]; IgG receptor activity [GO:0019770] | PF13895; | 2.60.40.10; | null | PTM: Phosphorylated by SRC-type Tyr-kinases such as LYN, BLK, FYN, HCK and SYK. {ECO:0000269|PubMed:8132624, ECO:0000269|PubMed:8756631}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19011614}; Single-pass type I membrane protein {ECO:0000269|PubMed:19011614}. | null | null | null | null | null | FUNCTION: Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens. Promotes phagocytosis of opsonized antigens. {ECO:0000269|PubMed:19011614}. | Homo sapiens (Human) |
P12319 | FCERA_HUMAN | MAPAMESPTLLCVALLFFAPDGVLAVPQKPKVSLNPPWNRIFKGENVTLTCNGNNFFEVSSTKWFHNGSLSEETNSSLNIVNAKFEDSGEYKCQHQQVNESEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYKVIYYKDGEALKYWYENHNISITNATVEDSGTYYCTGKVWQLDYESEPLNITVIKAPREKYWLQFFIPLLVVILFAVDTGLFISTQQQVTFLLKIKRTRKGFRLLNPHPKPNPKNN | null | null | cell surface receptor signaling pathway [GO:0007166]; eosinophil degranulation [GO:0043308]; immunoglobulin mediated immune response [GO:0016064]; mast cell degranulation [GO:0043303]; type 2 immune response [GO:0042092]; type I hypersensitivity [GO:0016068] | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | high-affinity IgE receptor activity [GO:0019768]; IgE binding [GO:0019863] | PF13895;PF13927; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8114916}; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: High-affinity receptor for immunoglobulin epsilon/IgE. Mediates IgE effector functions in myeloid cells. Upon IgE binding and antigen/allergen cross-linking initiates signaling pathways that lead to myeloid cell activation and differentiation. On mast cells, basophils and eosinophils stimulates the secretion ... | Homo sapiens (Human) |
P12333 | CB2A_SPIOL | MASSTMALSSPSLAGKAVKLGPTASEIIGEGRITMRKTAGKPKTVQSSSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFAKNRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWNFATNFVPGK | null | COFACTOR: Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin. {ECO:0000305|PubMed:15029188, ECO:0000305|PubMed:24482437}; | photosynthesis, light harvesting in photosystem I [GO:0009768]; response to light stimulus [GO:0009416] | chloroplast envelope [GO:0009941]; chloroplast thylakoid membrane [GO:0009535]; photosystem I [GO:0009522]; photosystem II [GO:0009523]; plastoglobule [GO:0010287] | chlorophyll binding [GO:0016168]; metal ion binding [GO:0046872] | PF00504; | 1.10.3460.10; | Light-harvesting chlorophyll a/b-binding (LHC) protein family | PTM: Photoregulated by reversible phosphorylation of its threonine residues. {ECO:0000269|PubMed:1894641}. | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. | Spinacia oleracea (Spinach) |
P12336 | GTR2_RAT | MSEDKITGTLAFTVFTAVLGSFQFGYDIGVINAPQEVIISHYRHVLGVPLDDRRATINYDINGTDTPLIVTPAHTTPDAWEEETEGSAHIVTMLWSLSVSSFAVGGMVASFFGGWLGDKLGRIKAMLAANSLSLTGALLMGCSKFGPAHALIIAGRSVSGLYCGLISGLVPMYIGEIAPTTLRGALGTLHQLALVTGILISQIAGLSFILGNQDYWHILLGLSAVPALLQCLLLLFCPESPRYLYLNLEEEVRAKKSLKRLRGTEDITKDINEMRKEKEEASTEQKVSVIQLFTDPNYRQPIVVALMLHLAQQFSGINGI... | null | null | carbohydrate utilization [GO:0009758]; cellular response to fatty acid [GO:0071398]; cellular response to organic cyclic compound [GO:0071407]; dehydroascorbic acid transport [GO:0070837]; fructose transmembrane transport [GO:0015755]; galactose transmembrane transport [GO:0015757]; glucose import [GO:0046323]; glucose... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; brush border [GO:0005903]; brush border membrane [GO:0031526]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; endosome [GO:0005768]; membrane [GO:0016020]; plasma membrane [GO:0005886] | D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; fructose transmembrane transporter activity [GO:0005353]; galactose transmembrane transporter activity [GO:0005354]; glucose transmembrane transporter activity [GO:0005355]; insulin receptor ... | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | PTM: N-glycosylated; required for stability and retention at the cell surface of pancreatic beta cells. {ECO:0000250|UniProtKB:P14246}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3048704}; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:3048704}; CATALYTIC ACTIVITY: Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372, ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:P11168}; CATALYTIC ACTIVITY: Reaction=L-dehy... | null | null | null | null | FUNCTION: Facilitative hexose transporter that mediates the transport of glucose, fructose and galactose (PubMed:3048704). Likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells; may comprise part of the glucose-sensing ... | Rattus norvegicus (Rat) |
P12337 | EST1_RABIT | MWLCALALASLAACTAWGHPSAPPVVDTVHGKVLGKFVSLEGFAQPVAVFLGVPFAKPPLGSLRFAPPQPAESWSHVKNTTSYPPMCSQDAVSGHMLSELFTNRKENIPLKFSEDCLYLNIYTPADLTKRGRLPVMVWIHGGGLMVGGASTYDGLALSAHENVVVVTIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALRWVQDNIANFGGDPGSVTIFGESAGGQSVSILLLSPLTKNLFHRAISESGVALLSSLFRKNTKSLAEKIAIEAGCKTTTSAVMVHCLRQKTEEELMEVTLKMKFMALDLVGDPKENTAFLTT... | 3.1.1.1 | null | lipid catabolic process [GO:0016042] | endoplasmic reticulum lumen [GO:0005788]; lipid droplet [GO:0005811] | carboxylesterase activity [GO:0106435] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=Microsomal membrane, lumen of endoplasmic reticulum. | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039}; | null | null | null | null | FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. {ECO:0000269|PubMed:9635592}. | Oryctolagus cuniculus (Rabbit) |
P12343 | AATC_RABIT | MAPPSIFAEVPQAQPVLVFKLTADFREDPDP | 2.6.1.1; 2.6.1.3 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | amino acid biosynthetic process [GO:0008652]; glycerol biosynthetic process [GO:0006114] | cytoplasm [GO:0005737] | L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-cysteine transaminase activity [GO:0047801] | null | null | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:4030726}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825; Evidence={ECO:0000250|U... | null | null | null | null | FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine (PubMed:4030726). Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involve... | Oryctolagus cuniculus (Rabbit) |
P12344 | AATM_BOVIN | MALLHSGRFLSGVAAAFHPGLAAAASARASSWWAHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIAGLAEFCKASAELALGENNEVLKSGRYVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPTWGNHTPIFRDAGMQLQSYRYYDPKTCGFDFTGAIEDISKIPAQSVILLHACAHNPTGVDPRPEQWKEMATVVKKNNLFAFFDMAYQGFASGDGNKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPMYSNPP... | 2.6.1.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; glutamate metabolic process [GO:0006536]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]; lipid transport [GO:0006869] | cell surface [GO:0009986]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate; Xref=Rhea... | null | null | null | null | FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid... | Bos taurus (Bovine) |
P12345 | AATM_RABIT | MALLHSARVLSGVASAFHPGLAAAASARASSWWAHVEMGPPDPILGVTEAYKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKGLDKEYLPIGGLAEFCRASAELALGENSEVVKSGRFVTVQTISGTGALRIGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQSYRYYDPKTCGFDFTGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIATVVKKRNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVICKDADEAKRVESQLKILIRPMYSNPP... | 2.6.1.1; 2.6.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; glutamate metabolic process [GO:0006536]; L-phenylalanine biosynthetic process from chorismate via phenylpyruvate [GO:0033585]; lipid transport [GO:0006869]; protein folding [GO:0006457] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; kynurenine-oxoglutarate transaminase activity [GO:0016212]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-tyrosine:2-oxoglutarate aminotransferase activity [GO:0004838]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Cell membrane {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000250|UniProtKB:P00507}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L... | null | null | null | null | FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid... | Oryctolagus cuniculus (Rabbit) |
P12346 | TRFE_RAT | MRFAVGALLACAALGLCLAVPDKTVKWCAVSEHENTKCISFRDHMKTVLPADGPRLACVKKTSYQDCIKAISGGEADAITLDGGWVYDAGLTPNNLKPVAAEFYGSLEHPQTHYLAVAVVKKGTDFQLNQLQGKKSCHTGLGRSAGWIIPIGLLFCNLPEPRKPLEKAVASFFSGSCVPCADPVAFPQLCQLCPGCGCSPTQPFFGYVGAFKCLRDGGGDVAFVKHTTIFEVLPQKADRDQYELLCLDNTRKPVDQYEDCYLARIPSHAVVARNGDGKEDLIWEILKVAQEHFGKGKSKDFQLFGSPLGKDLLFKDSAFG... | null | null | actin filament organization [GO:0007015]; acute-phase response [GO:0006953]; antibacterial humoral response [GO:0019731]; apoptotic process [GO:0006915]; cellular response to cAMP [GO:0071320]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to iron ion [GO:0071281]; ERK1 and ... | apical plasma membrane [GO:0016324]; basal part of cell [GO:0045178]; basal plasma membrane [GO:0009925]; basement membrane [GO:0005604]; cell surface [GO:0009986]; cell tip [GO:0051286]; clathrin-coated pit [GO:0005905]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; dense body [GO:0097433]; early endosome [... | ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; iron chaperone activity [GO:0034986]; transferrin receptor binding [GO:1990459] | PF00405; | 3.40.190.10; | Transferrin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a fur... | Rattus norvegicus (Rat) |
P12367 | KAP2_MOUSE | MSHIQIPPGLTELLQGYTVEVGQQPPDLVDFAVEYFTRLREARRQESDTFIVSPTTFHTQESSAVPVIEEDGESDSDSEDADLEVPVPSKFTRRVSVCAETFNPDEEEEDNDPRVVHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFEKIVKTDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIIATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLFKSLEMSERMKIVDVIGEKIYKDGERIIAQGEKADSFYIIESGEVSILIRSKTKSNKNGGNQ... | null | null | modulation of chemical synaptic transmission [GO:0050804]; regulation of protein phosphorylation [GO:0001932] | cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]; synapse [GO:0045202]; T-tubule [GO:0030315] | beta-2 adrenergic receptor binding [GO:0031698]; cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subun... | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: Phosphorylated by the activated catalytic chain. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. | Mus musculus (Mouse) |
P12368 | KAP2_RAT | MSHIQIPPGLTELLQGYTVEVLRQQPPDLVDFAVEYFTRLREARRQESDSFIAPPTTFHAQESSGVPVIEEDGESESDSDDEDLEVPIPSKFTRRVSVCAETFNPDEEEDNDPRVVHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFEKIVKTDEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSDGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLFKSLEMSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIRSKTKTNKNGGNQ... | null | null | modulation of chemical synaptic transmission [GO:0050804]; regulation of protein phosphorylation [GO:0001932] | cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nucleotide-activated protein kinase complex [GO:0031588]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; plasma membrane raft [GO:00... | beta-2 adrenergic receptor binding [GO:0031698]; cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subun... | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: Phosphorylated by the activated catalytic chain. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and the cell membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. | Rattus norvegicus (Rat) |
P12369 | KAP3_RAT | MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGAARFGHEGRTWGDAGAAAGGGTPSKGVNFAEEPMRSDSENGEEEEAAEAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVR... | null | null | fatty acid metabolic process [GO:0006631]; learning [GO:0007612]; modulation of chemical synaptic transmission [GO:0050804]; regulation of protein phosphorylation [GO:0001932]; response to antipsychotic drug [GO:0097332] | cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; perinuclear region... | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein domain specific binding [GO:0019904]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase binding [GO:0019901]; ubiquitin protein ligase bi... | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: Phosphorylated by the activated catalytic chain. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes with PJA2 in the cytoplasm and at the cell membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase. | Rattus norvegicus (Rat) |
P12370 | KAPC1_DROME | MGNNATTSNKKVDAAETVKEFLEQAKEEFEDKWRRNPTNTAALDDFERIKTLGTGSFGRVMIVQHKPTKDYYAMKILDKQKVVKLKQVEHTLNEKRILQAIQFPFLVSLRYHFKDNSNLYMVLEYVPGGEMFSHLRKVGRFSEPHSRFYAAQIVLAFEYLHYLDLIYRDLKPENLLIDSQGYLKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLVYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFGSDLKDLLRNLLQVDLTKRYGNLKAGVNDIKNQKWFASTDWIAIFQKKIEAPFIPR... | 2.7.11.11 | null | anesthesia-resistant memory [GO:0007615]; anterior/posterior pattern specification, imaginal disc [GO:0007448]; cAMP-mediated signaling [GO:0019933]; cellular response to ethanol [GO:0071361]; imaginal disc-derived wing morphogenesis [GO:0007476]; modulation of chemical synaptic transmission [GO:0050804]; negative regu... | cAMP-dependent protein kinase complex [GO:0005952]; cell body [GO:0044297]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; Evidence={ECO:0000305|PubMed:29473541}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase involved in memory formation (PubMed:29473541). Promotes long-term memory by phosphorylating meng and by regulating CrebB protein stability and activity (PubMed:29473541). As part of ethanol response in the glia, mediates ethanol-induced structural remodeling of actin cytoskele... | Drosophila melanogaster (Fruit fly) |
P12371 | FCERA_RAT | MDTGGSARLCLALVLISLGVMLTATQKSVVSLDPPWIRILTGDKVTLICNGNNSSQMNSTKWIHNDSISNVKSSHWVIVSATIQDSGKYICQKQGFYKSKPVYLNVMQEWLLLQSSADVVLDNGSFDIRCRSWKKWKVHKVIYYKDDIAFKYSYDSNNISIRKATFNDSGSYHCTGYLNKVECKSDKFSIAVVKDYTIEYRWLQLIFPSLAVILFAVDTGLWFSTHKQFESILKIQKTGKGKKKG | null | null | calcium-mediated signaling [GO:0019722]; cell surface receptor signaling pathway [GO:0007166]; eosinophil degranulation [GO:0043308]; establishment of localization in cell [GO:0051649]; immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064]; leukotriene biosynthetic process [GO:0019370]; mas... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | high-affinity IgE receptor activity [GO:0019768]; IgE binding [GO:0019863]; IgE receptor activity [GO:0019767] | PF13895; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12319}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted. | null | null | null | null | null | FUNCTION: High-affinity receptor for immunoglobulin epsilon/IgE. Mediates IgE effector functions in myeloid cells. Upon IgE binding and antigen/allergen cross-linking initiates signaling pathways that lead to myeloid cell activation and differentiation. On mast cells, basophils and eosinophils stimulates the secretion ... | Rattus norvegicus (Rat) |
P12382 | PFKAL_MOUSE | MATVDLEKLRMSGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVEGGENIKPANWLSVSNIIQLGGTIIGSARCKAFTTREGRLAAAYNLLQHGITNLCVIGGDGSLTGANIFRNEWGSLLEELVKEGKISESTAQNYAHLTIAGLVGSIDNDFCGTDMTIGTDSALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWENFMCERLGETRSRGSRLNIIIIAEGAIDRHGKPISSSYVKDLVVQRLGFDTRVTVLGHVQRGGTPSAFDRILSSKMGMEA... | 2.7.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; glycolytic process [GO:0006096]; glycolytic process through fructose-6-phosphate [GO:0061615]; negative regulation of insulin secretion [GO:0046676]; response to glucose [GO:... | 6-phosphofructokinase complex [GO:0005945]; cytosol [GO:0005829]; membrane [GO:0016020] | 6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; fructose binding [GO:0070061]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029] | PF00365; | 3.40.50.450;3.40.50.460; | Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Eukaryotic two domain clade 'E' sub-subfamily | PTM: GlcNAcylation at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}. | CATALYTIC ACTIVITY: Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03184}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_03184}. | null | null | FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis (By similarity). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by controlling cellular NADPH biosynthesis and NADPH oxidase-derived react... | Mus musculus (Mouse) |
P12383 | PDR1_YEAST | MRGLTPKNGVHIETGPDTESSADSSNFSTGFSGKIRKPRSKVSKACDNCRKRKIKCNGKFPCASCEIYSCECTFSTRQGGARIKNLHKTSLEGTTVQVKEETDSSSTSFSNPQRCTDGPCAVEQPTKFFENFKLGGRSSGDNSGSDGKNDDDVNRNGFYEDDSESQATLTSLQTTLKNLKEMAHLGTHVTSAIESIELQISDLLKRWEPKVRTKELATTKFYPNKSIETQLMKNKYCDVVHLTRYAAWSNNKKDQDTSSQPLIDEIFGLYSPFQFLSLQGIGKCFQNYRSKSKCEIFPRTAKETIYIMLRFFDVCFHHIN... | null | null | DNA-templated transcription [GO:0006351]; positive regulation of cellular response to drug [GO:2001040]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; zinc ion binding [GO:0008270] | PF04082;PF00172; | 4.10.240.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Positive regulator of proteins involved in permeability. PDR1 and PDR3 jointly control the transcription level of both SNQ2 and PDR5. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12385 | ERF1_YEAST | MDNEVEKNIEIWKVKKLVQSLEKARGNGTSMISLVIPPKGQIPLYQKMLTDEYGTASNIKSRVNRLSVLSAITSTQQKLKLYNTLPKNGLVLYCGDIITEDGKEKKVTFDIEPYKPINTSLYLCDNKFHTEVLSELLQADDKFGFIVMDGQGTLFGSVSGNTRTVLHKFTVDLPKKHGRGGQSALRFARLREEKRHNYVRKVAEVAVQNFITNDKVNVKGLILAGSADFKTDLAKSELFDPRLACKVISIVDVSYGGENGFNQAIELSAEALANVKYVQEKKLLEAYFDEISQDTGKFCYGIDDTLKALDLGAVEKLIVF... | null | null | cytoplasmic translational termination [GO:0002184]; DNA-templated transcription termination [GO:0006353]; translational termination [GO:0006415] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; translation release factor complex [GO:0018444] | aminoacyl-tRNA hydrolase activity [GO:0004045]; sequence-specific mRNA binding [GO:1990825]; translation release factor activity [GO:0003747]; translation release factor activity, codon specific [GO:0016149] | PF03463;PF03464;PF03465; | 3.30.1330.30;3.30.960.10;3.30.420.60; | Eukaryotic release factor 1 family | PTM: N5-methylated on Gln-182 by MTQ2. {ECO:0000269|PubMed:15509572, ECO:0000269|PubMed:16321977}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons (PubMed:20947765, PubMed:34413231, PubMed:7556078). The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:20947765, PubMed:7556078). SUP45/eRF... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12387 | CO3_CAVPO | MGPAAGPSLLLLLLASVSLALGDPMYSIITPNILRLENEETVVLEAHEVQGDIPVTVTVHDFPAKKNVLSSEKTVLTSATGYLGTVTIKIPASKEFKSDKGRKLVVVQAAFGGTQLEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVDSDLLPVGRTIIVTIETPDGIPIKRDTLSSNNQHGILPLSWNIPELVNMGQWKIQAFYENSPKQVFSAEFEVKEYVLPSFEVLVEPTEKFYYIDDPKGLEVNIIARFLYGKNVDGTAFVIFGVQDGDQRISLAQSLTRVVIEDGSGEVVLSRQVLLDGVQPSRPEALVG... | null | null | complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; inflammatory response [GO:0006954]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation o... | extracellular space [GO:0005615] | C5L2 anaphylatoxin chemotactic receptor binding [GO:0031715]; endopeptidase inhibitor activity [GO:0004866] | PF00207;PF07703;PF07677;PF01821;PF21406;PF21308;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678; | 1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10; | null | PTM: C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.; FUNCTION... | Cavia porcellus (Guinea pig) |
P12388 | PAI2_MOUSE | MEELSMANTMFALNLLKQIEKSNSTQNIFISPWSISSTLAIVLLGAGGNTEQQMAKVLQFNEIGSYGITTRNPENFSGCDFAQQIQKENYPSAILQAQAGDKIHSAFSSLSSTINTPQGDYLLESANKLFGEKSARFKEEYIQLSKKYYSTEPEAVDFLECAEEAREKINSWVKTQTKGEIPNLLPEGSVDEDTKMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSHESIPVQMMFLHAKLNIGYIKDLKTQILELPHTGNISMLLLLPDEIEDASTGLELLESEINFANFNKWISKDTLDEDDVVVYIPKFKLAQSYEL... | null | null | negative regulation of apoptotic process [GO:0043066] | cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family, Ov-serpin subfamily | PTM: The signal sequence is not cleaved. | SUBCELLULAR LOCATION: Cytoplasm. Secreted, extracellular space. | null | null | null | null | null | FUNCTION: Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1. Not required for normal murine development or survival. | Mus musculus (Mouse) |
P12389 | ACHA2_RAT | MTLSHSALQFWTHLYLWCLLLVPAVLTQQGSHTHAEDRLFKHLFGGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWNDYKLRWDPAEFGNVTSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFFTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMERTVDLKDYWESGEWAIINATGTYNSKKYDCCAEIYPDVTYYFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSI... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; cellular response to nicotine [GO:0071316]; membrane depolarization [GO:0051899]; modulation of inhibitory postsynaptic potential [GO:0098828]; response to acetylcholine [GO:1905144]; response to nicotine [GO:0035094]; signal transduction [GO:0007165]; synaptic tra... | acetylcholine-gated channel complex [GO:0005892]; cell periphery [GO:0071944]; intercellular bridge [GO:0045171]; neuron projection [GO:0043005]; neuron projection cytoplasm [GO:0120111]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; protein-containing complex [GO:0032991];... | acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; heterocyclic compound binding [GO:1901363]; quaternary ammonium group binding [GO:0050997] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-2/CHRNA2 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. | Rattus norvegicus (Rat) |
P12390 | ACHB2_RAT | MAGHSNSMALFSFSLLWLCSGVLGTDTEERLVEHLLDPSRYNKLIRPATNGSELVTVQLMVSLAQLISVHEREQIMTTNVWLTQEWEDYRLTWKPEDFDNMKKVRLPSKHIWLPDVVLYNNADGMYEVSFYSNAVVSYDGSIFWLPPAIYKSACKIEVKHFPFDQQNCTMKFRSWTYDRTEIDLVLKSDVASLDDFTPSGEWDIIALPGRRNENPDDSTYVDITYDFIIRRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLDVPLVGKYLMFTMVLVTFSIVTSVCVLNV... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; action potential [GO:0001508]; associative learning [GO:0008306]; B cell activation [GO:0042113]; B cell proliferation [GO:0042100]; behavioral response to nicotine [GO:0035095]; calcium ion transport [GO:0006816]; central nervous system neuron axonogenesis [GO:002... | acetylcholine-gated channel complex [GO:0005892]; cholinergic synapse [GO:0098981]; dopaminergic synapse [GO:0098691]; external side of plasma membrane [GO:0009897]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; postsynaptic specialization membrane [GO:0099634]; presyn... | acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; heterocyclic compound binding [GO:1901363]; protein-containing complex binding [GO:0044877]; quaternary ammonium group binding [GO:0050997]; transmitter-gated ... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Beta-2/CHRNB2 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodiun ions. | Rattus norvegicus (Rat) |
P12391 | ACHB3_RAT | MTGFLRVFLVLSATLSGSWVTLTATAGLSSVAEHEDALLRHLFQGYQKWVRPVLNSSDIIKVYFGLKISQLVDVDEKNQLMTTNVWLKQEWTDQKLRWNPEEYGGINSIKVPSESLWLPDIVLFENADGRFEGSLMTKAIVKSSGTVSWTPPASYKSSCTMDVTFFPFDRQNCSMKFGSWTYDGTMVDLILINENVDRKDFFDNGEWEILNAKGMKGNRREGFYSYPFVTYSFVLRRLPLFYTLFLIIPCLGLSFLTVLVFYLPSDEGEKLSLSTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYLLFIMIFVTLSIIVT... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; response to nicotine [GO:0035094]; synaptic transmission, cholinergic [GO:0007271] | acetylcholine-gated channel complex [GO:0005892]; dopaminergic synapse [GO:0098691]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynapse [GO:0098793]; protein-containing complex [GO:0032991]; synapse [GO:0045202] | acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Beta-3/CHRNB3 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. | Rattus norvegicus (Rat) |
P12392 | ACHB4_RAT | MRGTPLLLVSLFSLLQDGDCRLANAEEKLMDDLLNKTRYNNLIRPATSSSQLISIRLELSLSQLISVNEREQIMTTSIWLKQEWTDYRLAWNSSCYEGVNILRIPAKRVWLPDIVLYNNADGTYEVSVYTNVIVRSNGSIQWLPPAIYKSACKIEVKHFPFDQQNCTLKFRSWTYDHTEIDMVLKSPTAIMDDFTPSGEWDIVALPGRRTVNPQDPSYVDVTYDFIIKRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTFFLLLISKIVPPTSLDIPLIGKYLLFTMVLVTFSIVTTVCVLNVHH... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; behavioral response to nicotine [GO:0035095]; locomotory behavior [GO:0007626]; membrane depolarization [GO:0051899]; neuronal action potential [GO:0019228]; positive regulation of transmission of nerve impulse [GO:0051971]; regulation of membrane potential [GO:004... | acetylcholine-gated channel complex [GO:0005892]; cholinergic synapse [GO:0098981]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; protein-containing complex [GO:0032991]; synapse [GO:0045202] | acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; heterocyclic compound binding [GO:1901363]; protein-containing complex binding [GO:0044877]; transmitter-gated monoatomic ion channel activity involved in regu... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Beta-4/CHRNB4 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. | Rattus norvegicus (Rat) |
P12411 | TBB1_ARATH | MREILHVQGGQCGNQIGSKFWEVICDEHGVDPTGRYNGDSADLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSIRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDAVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLSTPSFGDLNHLISATMSGVTCSLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYISLTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRG... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; response to light stimulus [GO:0009416]; unidimensional cell growth [GO:0009826] | microtubule [GO:0005874]; vacuole [GO:0005773] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Arabidopsis thaliana (Mouse-ear cress) |
P12412 | CYSEP_VIGMU | MAMKKLLWVVLSLSLVLGVANSFDFHEKDLESEESLWDLYERWRSHHTVSRSLGEKHKRFNVFKANVMHVHNTNKMDKPYKLKLNKFADMTNHEFRSTYAGSKVNHHKMFRGSQHGSGTFMYEKVGSVPASVDWRKKGAVTDVKDQGQCGSCWAFSTIVAVEGINQIKTNKLVSLSEQELVDCDKEENQGCNGGLMESAFEFIKQKGGITTESNYPYTAQEGTCDESKVNDLAVSIDGHENVPVNDENALLKAVANQPVSVAIDAGGSDFQFYSEGVFTGDCNTDLNHGVAIVGYGTTVDGTNYWIVRNSWGPEWGEQGY... | 3.4.22.- | null | proteolysis involved in protein catabolic process [GO:0051603] | aleurone grain [GO:0033095]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | PTM: The mature protein is not glycosylated.; PTM: The precursor stored in the endoplasmic reticulum lumen is processed during the transport to proteins bodies to two dominant mature forms that differ by a single amino acid residue at the N-terminus. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:8076688}. Vacuole, aleurone grain {ECO:0000269|PubMed:8076688}. | null | null | null | null | null | FUNCTION: Thought to be involved in the hydrolysis of stored seed proteins. In vitro, catalyzes the hydrolysis of proteins, such as azocasein. Shows a preferential cleavage for Asn-|-Xaa in small molecule substrates such as Boc-Asn-|-OPHNO(2). | Vigna mungo (Black gram) (Phaseolus mungo) |
P12425 | GLN1A_BACSU | MAKYTREDIEKLVKEENVKYIRLQFTDILGTIKNVEIPVSQLGKALDNKVMFDGSSIEGFVRIEESDMYLYPDLNTFVIFPWTAEKGKVARFICDIYNPDGTPFEGDPRNNLKRILKEMEDLGFSDFNLGPEPEFFLFKLDEKGEPTLELNDKGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYAGAVRSCDDIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHCNLSLFKNGVNAFFDENADLQLSETAKHFIAGIVKHATSFTAVTNPTVNSYKRLVPGYEAPCYVAWSAQNRSPLI... | 6.3.1.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24158439, ECO:0000269|PubMed:25691471}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:24158439, ECO:0000269|PubMed:25691471}; | cellular response to nitrogen levels [GO:0043562]; glutamine biosynthetic process [GO:0006542]; negative regulation of core promoter binding [GO:1904797]; negative regulation of DNA-templated transcription [GO:0045892]; nitrogen catabolite repression of transcription [GO:0090295]; polyamine catabolic process [GO:000659... | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; glutamate binding [GO:0016595]; glutamine binding [GO:0070406]; glutamine synthetase activity [GO:0004356]; magnesium ion binding [GO:0000287] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17001076}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:12139611, ECO:0000269|PubMe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.18 mM for ammonium {ECO:0000269|PubMed:24158439}; KM=0.83 mM for hydroxylamine {ECO:0000269|PubMed:24158439}; KM=2.3 mM for ATP {ECO:0000269|PubMed:12139611}; KM=2.4 mM for ATP {ECO:0000269|PubMed:24158439}; KM=12 mM for glutamine {ECO:0000269|PubMed:12139611}; K... | null | null | null | FUNCTION: Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism (PubMed:25691471). It catalyzes the ATP-dependent biosynthesis of glutamine from glutam... | Bacillus subtilis (strain 168) |
P12428 | BROWN_DROME | MQESGGSSGQGGPSLCLEWKQLNYYVPDQEQSNYSFWNECRKKRELRILQDASGHMKTGDLIAILGGSGAGKTTLLAAISQRLRGNLTGDVVLNGMAMERHQMTRISSFLPQFEINVKTFTAYEHLYFMSHFKMHRRTTKAEKRQRVADLLLAVGLRDAAHTRIQQLSGGERKRLSLAEELITDPIFLFCDEPTTGLDSFSAYSVIKTLRHLCTRRRIAKHSLNQVYGEDSFETPSGESSASGSGSKSIEMEVVAESHESLLQTMRELPALGVLSNSPNGTHKKAAICSIHQPTSDIFELFTHIILMDGGRIVYQGRTEQ... | 7.6.2.-; 7.6.2.6 | null | aminergic neurotransmitter loading into synaptic vesicle [GO:0015842]; eye pigment precursor transport [GO:0006856]; guanine transport [GO:0015854]; sensory perception of sound [GO:0007605]; transmembrane transport [GO:0055085] | plasma membrane [GO:0005886]; presynapse [GO:0098793] | ABC-type transporter activity [GO:0140359]; amine transmembrane transporter activity [GO:0005275]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; guanine transmembrane transporter activity [GO:0015208]; pigment binding [GO:0031409] | PF01061;PF19055;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family, Eye pigment precursor importer (TC 3.A.1.204) subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + guanine(out) + H2O = ADP + guanine(in) + H(+) + phosphate; Xref=Rhea:RHEA:20832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16235, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.6.2.6; Evidence={ECO:0000305|PubMed:117796}; CATALYTIC ACTIVITY: Reaction=ATP + H2O ... | null | null | null | null | FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family which transports various molecules including bioamines, neurotransmitters and metabolic intermediates (PubMed:10407069, PubMed:117796, PubMed:18931318, PubMed:33820991, PubMed:8144619). In the eye and probably in association with w/white, requ... | Drosophila melanogaster (Fruit fly) |
P12429 | ANXA3_HUMAN | MASIWVGHRGTVRDYPDFSPSVDAEAIQKAIRGIGTDEKMLISILTERSNAQRQLIVKEYQAAYGKELKDDLKGDLSGHFEHLMVALVTPPAVFDAKQLKKSMKGAGTNEDALIEILTTRTSRQMKDISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKQDAQILYKAGENRWGTDEDKFTEILCLRSFPQLKLTFDEYRNISQKDIVDSIKGELSGHFEDLLLAIVNCVRNTPAFLAERLHRALKGIGTDEFTLNRIMVSRSEIDLLDIRTEFKKHYGYSLYSAIKSDTSGDYEITLLKICG... | null | null | animal organ regeneration [GO:0031100]; defense response to bacterium [GO:0042742]; hippocampus development [GO:0021766]; neutrophil degranulation [GO:0043312]; phagocytosis [GO:0006909]; positive regulation of angiogenesis [GO:0045766]; positive regulation of DNA metabolic process [GO:0051054]; positive regulation of ... | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; specific granule [GO:0042581] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834] | PF00191; | 1.10.220.10; | Annexin family | null | null | null | null | null | null | null | FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. | Homo sapiens (Human) |
P12449 | ENV_HV2SB | MSGKIQLLVAFLLTSACLIYCTKYVTVFYGVPVWKNASIPLFCATKNRDTWGTIQCLPDNDDYQEIPLNVTEAFDAWDNIVTEQAVEDVWNLFETSIKPCVKLTPLCVTMNCNASTESAVATTSPSGPDMINDTDPCIQLNNCSGLREEDMVECQFNMTGLELDKKKQYSETWYSKDVVCESDNSTDRKRCYMNHCNTSVITESCDKHYWDAMRFRYCAPPGFVLLRCNDTNYSGFEPNCSKVVASTCTRMMETQPSTWLGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTILCRRPENKTVVPITLMSGRRFHSQKI... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy a... | Human immunodeficiency virus type 2 subtype A (isolate SBLISY) (HIV-2) |
P12450 | GAG_HV2SB | MGAKNSVLRGKKADELEKIRLRPGGKKKYRLKHIVWAANELDRFGLTESLLESKEGCQKIISVLEPLVPTGSENLKSLYNTTCVIWCLHAEEKVKDTEEAKRIVGRHLVAETETAEKMPNISRPTAPPSGKGGNFPVQQIGGNYVHLPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDVQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIEWMYRQENPVPVGNIYRRWIQIGLQKCVRMYNPTNILDIKQGPKESFQSYVDRFYKSLRAEQTDAAVKNWMT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate SBLISY) (HIV-2) |
P12451 | POL_HV2SB | MGAKNSVLRGKKADELEKIRLRPGGKKKYRLKHIVWAANELDRFGLTESLLESKEGCQKIISVLEPLVPTGSENLKSLYNTTCVIWCLHAEEKVKDTEEAKRIVGRHLVAETETAEKMPNISRPTAPPSGKGGNFPVQQIGGNYVHLPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDVQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIEWMYRQENPVPVGNIYRRWIQIGLQKCVRMYNPTNILDIKQGPKESFQSYVDRFYKSLRAEQTDAAVKNWMT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immun... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate SBLISY) (HIV-2) |
P12456 | TBB1_CAEEL | MREIVHIQAGQCGNQIGSKFWEVISDEHGIDPSGQYVGDSDLQLERINVYYNEAGSNKYVPRAVLVDLEPGTMDSVRSGPFGQLFRPDNYVFGQSGAGNNWAKGHYTEGAELVDNVLDVVRKEAESTDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDSTFCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRSNQQYRAITVPELTQQCFDAKNMMAACDPRHGRYLTAAAIFRGR... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | cytoplasmic microtubule organization [GO:0031122]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; detection of mechanical stimulus involved in sensory perception of touch [GO:0050976]; mechanosensory behavior [GO:0007638]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell c... | cytoplasm [GO:0005737]; microtubule [GO:0005874]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: TTubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers ... | Caenorhabditis elegans |
P12473 | VP4_ROTRH | MASLIYRQLLTNSYTVDLSDEIQEIGSTKTQNVTINLGPFAQTGYAPVNWGPGETNDSTTVEPVLDGPYQPTSFNPPVDYWMLLAPTAAGVVVEGTNNTDRWLATILVEPNVTSETRSYTLFGTQEQITIANASQTQWKFIDVVKTTQNGSYSQYGPLQSTPKLYAVMKHNGKIYTYNGETPNVTTKYYSTTNYDSVNMTAFCDFYIIPREEESTCTEYINNGLPPIQNTRNIVPLALSARNIISHRAQANEDIVVSKTSLWKEMQYNRDITIRFKFASSIVKSGGLGYKWSEISFKPANYQYTYTRDGEDVTAHTTCSV... | null | null | permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell plasma membrane [GO:0020002]; host cell rough endoplasmic reticulum [GO:0044168]; host cytoskeleton [GO:0044163]; membrane [GO:0016020]; viral outer capsid [GO:0039624] | null | PF17477;PF00426;PF17478; | 1.20.5.170;2.60.120.200; | Rotavirus VP4 family | PTM: [Outer capsid protein VP4]: Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion (PubMed:8709201, PubMed:9... | SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:15329727, ECO:0000269|PubMed:29263265}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04132}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:29263265}. Host cytoplasm, hos... | null | null | null | null | null | FUNCTION: [Outer capsid protein VP4]: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence (PubMed:25211455). Rotavirus attachment and entry into the host cell probably involves multi... | Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A) |
P12476 | VP7_ROTRH | MYGIEYTTVLTFLISLILLNYILKSLTRMMDFIIYRFLFIVVILSPLLKAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTDIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDTATFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDVLDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVNQIIQAMSKRSRSLNSA... | null | null | receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum lumen [GO:0044166]; T=13 icosahedral viral capsid [GO:0039621]; viral outer capsid [GO:0039624] | metal ion binding [GO:0046872] | PF00434; | 3.40.50.11130;2.60.120.800; | Rotavirus VP7 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:8035518}.; PTM: The N-terminus is blocked possibly by pyroglutamic acid. {ECO:0000255|HAMAP-Rule:MF_04131}. | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:19487668, ECO:0000269|PubMed:19520960, ECO:0000269|PubMed:21157433, ECO:0000269|PubMed:2832610}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. ... | null | null | null | null | null | FUNCTION: Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. Following entry int... | Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A) |
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