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A protein complex composed of three identical PCNA monomers, each comprising two similar domains, which are joined in a head-to-tail arrangement to form a homotrimer. Forms a ring-like structure in solution, with a central hole sufficiently large to accommodate the double helix of DNA. Originally characterized as a DNA sliding clamp for replicative DNA polymerases and as an essential component of the replisome, and has also been shown to be involved in other processes including Okazaki fragment processing, DNA repair, translesion DNA synthesis, DNA methylation, chromatin remodeling and cell cycle regulation. A protein complex that contains the precursor form of NF-kappaB (p105), the NF-kappaB inhibitor ABIN-2, and the kinase TPL-2 (MAP3K8); the complex stabilizes TPL-2 and is involved in signaling in lipopolysaccharide (LPS)-stimulated macrophages. A protein complex that has protein serine/threonine phosphatase activity that is polycation-stimulated (PCS), being directly stimulated by protamine, polylysine, or histone H1; it constitutes a subclass of several enzymes activated by different histones and polylysine, and consists of catalytic, scaffolding, and regulatory subunits. The catalytic and scaffolding subunits form the core enzyme, and the holoenzyme also includes the regulatory subunit. An integral membrane complex that possesses NADH oxidoreductase activity. The complex is one of the components of the electron transport chain. It catalyzes the transfer of a pair of electrons from NADH to a quinone. A complex formed by a recombinase, a regulatory protein, and the DNA sequences bound by each protein; catalyzes a reversible site-specific recombination reaction that results in the alternate expression of one or more genes in various contexts. A heterodimeric protein complex formed of BRCA2 and MAGE-D1; may mediate the synergistic activities of the two proteins in regulating cell growth. A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates. Any complex that acts to move proteins or RNAs into or out of the nucleus through nuclear pores. The living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm. A heterohexameric protein complex that is involved in tRNA modification, and exerts indirect effects on transcriptional elongation and exocytosis. The complex can associate physically with hyperphosphorylated RNA polymerase II; it contains two discrete heterotrimeric subcomplexes. A protein complex that contains the TOR (target of rapamycin) serine/threonine kinase and mediates temporal control of cell growth via regulation of translation, transcription, ribosome biogenesis, nutrient transport, and autophagy. In Saccharomyces, the complex contains Kog1p, Lst8p, Tco89p, and either Tor1p or Tor2p; in mammals the complex contains orthologs of the yeast proteins. The inner, i.e. lumen-facing, lipid bilayer of an organelle envelope; usually highly selective to most ions and metabolites. A protein complex that contains the TOR (target of rapamycin) serine/threonine kinase and mediates spatial control of cell growth via regulation of actin cytoskeleton polarization. In Saccharomyces, the complex contains Avo1p, Avo2p, Tsc11p, Lst8p, Bit61p, Slm1p, Slm2p, and Tor2p; in mammals the complex contains orthologs of the yeast proteins. A complex of multiple copies of three enzymatic components: oxoglutarate dehydrogenase (lipoamide) ; EC:1.2.4.2 (E1), dihydrolipoamide S-succinyltransferase ; EC:2.3.1.61 (E2) and dihydrolipoamide dehydrogenase ; EC:1.8.1.4 (E3); catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and carbon dioxide (CO2). Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and one B subunit bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between subunit B and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap. A protein complex containing an I-kappaB protein and one or more copies of an NF-kappaB protein; mediates regulation of NF-kappaB activity by I-kappaB. A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient. Any complex that possesses RNA polymerase activity; generally comprises a catalytic subunit and one or more additional subunits. A protein complex that contains the mTOR (mammalian target of rapamycin) serine/threonine kinase and the peptidyl-prolyl cis-trans isomerase FKBP12 (FKBP1A). A protein complex that possesses AMP-dependent protein kinase activity. A protein complex proposed to be involved in transcription as well as promoting telomere uncapping and telomere elongation. For example, in Saccharomyces cerevisiae the complex contains Bud32p, Kae1p, Gon7p, Cgi121p, and Pcc1p. A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms. The lipid bilayer surrounding an attachment organelle. A heterodimeric protein complex required for the activation of DNA replication origins; comprises a catalytic subunit and a regulatory subunit (in Saccharomyces, Cdc7p and Dbf4p, respectively); complexes identified in other species generally contain proteins related to the Saccharomyces proteins. A ferritin complex located in the cell. Intracellular ferritin complexes contain 24 subunits, in a mixture of L (light) chains and H (heavy) chains. Complex that possesses NAD(P)H dehydrogenase (plastoquinone) activity. The complex is one of the components of the electron transport chain. It is involved in electron transport from an unidentified electron donor, possibly NADH, NADPH or ferredoxin(Fd) to the plastoquinone pool. The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled. Any constituent part of the living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm. An enzyme complex that catalyzes the oxidation of reduced ferredoxin. Hydrogenase contains iron-sulfur clusters, and some contain nickel; it can use molecular hydrogen for the reduction of a variety of substances. One of two stalks that connect the catalytic core of the hydrogen-transporting ATP synthase to the membrane-associated Fo proteins; is thought to prevent futile rotation of the catalytic core. All non-F1 subunits of a hydrogen-transporting ATP synthase, including integral and peripheral membrane proteins. A protein complex that possesses NAD(P)+ transhydrogenase (AB-specific) activity. Homodimeric, trimeric, and heterotetrameric complexes have been identified. The hexamer that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase. A complex that catalyzes the transfer of an acetyl group to a protein acceptor molecule. A protein complex that mediates the conversion of a Holliday junction into two separate duplex DNA molecules; the complex includes a single- or multisubunit helicase that catalyzes the extension of heteroduplex DNA by branch migration and a nuclease that resolves the junction by nucleolytic cleavage. One of two stalks that connect the catalytic core of the hydrogen-transporting ATP synthase to the membrane-associated Fo proteins; rotates within the catalytic core during catalysis. Complex of 3'-5' exoribonucleases. A protein complex that contains the transforming acidic coiled coil (TACC) protein and the TOG protein (Mia1p/Alp7p and Alp14, respectively, in fission yeast), and is involved in microtubule array remodeling as cells progress through the cell cycle. The TACC/TOG complex is conserved in eukaryotes, associates with microtubules, and shuttles between the nucleus and the cytoplasm during interphase. A protein complex that possesses DNA polymerase activity and is involved in template directed synthesis of DNA. A protein complex that transfers electrons from ubiquinol to cytochrome c and translocates two protons across a membrane. The complex contains a core structure of three catalytic subunits: cytochrome b, the Rieske iron sulfur protein (ISP), and cytochrome c1, which are arranged in an integral membrane-bound dimeric complex; additional subunits are present, and vary among different species. A membranous cellular structure that bears the photosynthetic pigments in plants, algae, and cyanobacteria. In cyanobacteria thylakoids are of various shapes and are attached to, or continuous with, the plasma membrane. In eukaryotes they are flattened, membrane-bounded disk-like structures located in the chloroplasts; in the chloroplasts of higher plants the thylakoids form dense stacks called grana. Isolated thylakoid preparations can carry out photosynthetic electron transport and the associated phosphorylation. A part of the respiratory chain, containing the 13 polypeptide subunits of cytochrome c oxidase, including cytochrome a and cytochrome a3. Catalyzes the oxidation of reduced cytochrome c by dioxygen (O2). A part of the respiratory chain, containing the four polypeptide subunits of succinate dehydrogenase, flavin-adenine dinucleotide and iron-sulfur. Catalyzes the oxidation of succinate by ubiquinone. Connects the TCA cycle with the respiratory chain. Any complex that possesses ubiquitin conjugating enzyme activity. A multiprotein complex that binds microtubules in a Hedgehog-dependent manner, and is required for signal transduction by members of the Hedgehog family of proteins. The core components of the complex are the serine/threonine protein kinase Fused, the kinesin motor protein Costal2 (Cos2), and a zinc finger transcription factor (Gli family members in humans, and Cubitus interruptus (Ci) in Drosophila). A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex. A multisubunit complex, which caps one or both ends of the proteasome core complex. This complex recognizes and unfolds ubiquitinated proteins, and translocates them to the proteasome core complex. An enzyme complex that catalyzes exonucleolytic cleavage in either 5' to 3' or 3' to 5' direction to yield nucleoside 5'-phosphates; it prefers single-stranded DNA. A discrete intracellular part formed of aggregated molecules such as proteins or other biopolymers. The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope. The part of a cell or its extracellular environment in which a gene product is located. A gene product may be located in one or more parts of a cell and its location may be as specific as a particular macromolecular complex, that is, a stable, persistent association of macromolecules that function together. A protein complex that possesses methyltransferase activity. Any complex formed of proteins that act in mismatch repair. A protein complex with ubiquitin ligase activity that is involved in proteasomal degradation of fructose-1,6-bisphosphatase (FBPase) and phosphoenolpyruvate carboxykinase during the transition from gluconeogenic to glycolytic growth conditions. In S. cerevisiae, the GID (Glucose Induced degradation Deficient) complex consists of Vid30p, Rmd5p, Vid24p, Vid28p, Gid7p, Gid8p, and Fyv10p. A cytoplasmic part that appears as an electron-dense sphere of around 1.5 micron diameter containing Yb protein found in somatic cells of ovary and testis. There are one to two Yb bodies per cell. A protein complex formed by the association of superoxide dismutase 1 (SOD1) with calcineurin; complex formation is implicated in activation of calcineurin by SOD1. A protein complex that acts as an aryl hydrocarbon (Ah) receptor. Cytosolic and nuclear Ah receptor complexes have different subunit composition, but both contain the ligand-binding subunit AhR. A membrane-bound flavoenzyme complex consisting of four subunits, A, B, C, and D. A and B comprise the membrane-extrinsic catalytic domain and C (InterPro:IPR003510; InterPro:IPR004224) and D (InterPro:IPR003418) link the catalytic centers to the electron-transport chain. This family consists of the 13 kDa hydrophobic subunit D. This component may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalyzed by the related complex II of the respiratory chain (succinate dehydrogenase-(ubiquinone)). A subcomplex of DNA polymerase III composed of the epsilon subunit which has proofreading activity, and the theta subunit which enhances the epsilon subunit's proofreading activity. A heptamer that includes the tau and gamma products of the dnaX gene and the chi/psi subcomplex. Confers structural asymmetry that allows the polymerase to replicate both leading and lagging strands. A multimeric enzyme complex composed of variable numbers of catalytic alpha subunits, and noncatalytic beta subunits. The beta subunits are believed to have a regulatory function. The enzyme complex catalyzes the synthesis of S-adenosylmethionine (AdoMet), which is the major methyl group donor, participating in the methylation of proteins, DNA, RNA, phospholipids, and other small molecules. A multimeric complex which consists of flavoprotein (subunit A ; InterPro:IPR003952), iron-sulfur protein (subunit B) and membrane-bound cytochrome b560 (subunit C; InterPro:IPR000701). In some Archaea, the membrane-bound subunits (C or C and D) do not necessarily contain heme. Membrane-bound subunits can bind or react with quinones. A dimer composed of the chi and psi subunits which is a subassembly of the DNA polymerase III DnaX complex and serves as a bridge between the DnaX complex and the single-stranded DNA-binding protein (SSB). A protein complex that possesses ribonuclease H activity, in which the catalytic subunit is a member of the RNase H2 (or HII) class. For example, in Saccharomyces the complex contains Rnh201p, Rnh202p and Rnh203p. A protein complex formed by the association of the guanine nucleotide exchange factor synembrin with the alpha(i)1 subunit of a heterotrimeric G protein. A protein complex formed by the association of the guanine nucleotide exchange factor synembrin with the alpha(13) subunit of a heterotrimeric G protein. A protein complex formed by the association of the guanine nucleotide exchange factor synembrin with the alpha(q) subunit of a heterotrimeric G protein. A protein complex formed by the association of the guanine nucleotide exchange factor synembrin with the alpha(o) subunit of a heterotrimeric G protein. The lipid bilayer surrounding a microneme. The portion of the budding yeast plasma membrane where a daughter cell will emerge. The yeast marks this spot with bud-site selection proteins before bud emergence occurs. Actin is polarized to this spot just prior to and during bud emergence. A protein complex that consists of a homo- or heterodimer of members of a family of structurally related proteins that contain a conserved N-terminal region called the Rel homology domain (RHD). In the nucleus, NF-kappaB complexes act as transcription factors. In unstimulated cells, NF-kappaB dimers are sequestered in the cytoplasm by IkappaB monomers; signals that induce NF-kappaB activity cause degradation of IkappaB, allowing NF-kappaB dimers to translocate to the nucleus and induce gene expression. An immotile primary cilium that is found at the apical surface of auditory receptor cells. The kinocilium is surrounded by actin-based stereocilia. A complex that possesses glutamate synthase activity. A protein complex containing Bcl3 and Bcl10, which forms when Akt1 is activated by TNF-alpha to phosphorylate Bcl10; the Bcl3-Bcl10 complex is translocated to the nucleus. Organized structure of distinctive morphology and function, occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton. Excludes the plasma membrane. An intracellular part that represents the innermost portion of an endospore; the endospore core is dehydrated, enriched in dipicolinic acid and divalent cations, and metabolically inactive. The outer, i.e. cytoplasm-facing in a cellular organelle, lipid bilayer of an organelle envelope. A large multisubunit complex which catalyzes protein degradation. This complex consists of the barrel shaped proteasome core complex and one or two associated proteins or complexes that act in regulating entry into or exit from the core. Complex that possesses DNA topoisomerase (ATP-hydrolyzing) activity. A protein complex that possesses DNA helicase activity. A protein complex that consists of SMAD proteins; may be homomeric or heteromeric. The bundle of microtubules and associated proteins that forms the core of cilia and flagella in eukaryotic cells and is responsible for their movements. An actin-based protrusion from the apical surface of auditory and vestibular hair cells. Bundles of stereocilia act as mechanosensory organelles. A multisubunit iron flavoprotein, which in yeast is composed of 2 alpha and 2 beta subunits. Catalyzes the reduction of sulfite to sulfide. An enzyme complex that catalyzes exonucleolytic cleavage (in the presence of ATP) in either 5' to 3' or 3' to 5' direction to yield 5'-phosphooligonucleotides. Exodeoxyribonuclease V shows a preference for double-stranded DNA and possesses DNA-dependent ATPase activity. It acts endonucleolytically on single-stranded circular DNA. A protein complex that consists of the DNA binding protein TEAD-2 bound to 12 other polypeptides including the transcriptional coactivator YAP, the multi-PDZ domain protein MPDZ (also called MUPP1), a 14-3-3 domain protein, and others. Loosely bound to the surface of the plasma membrane that faces the cytoplasm, but not integrated into the hydrophobic region. Cyclin-dependent protein kinases (CDKs) are heterodimeric enzymes that contain a kinase catalytic subunit associated with a regulatory cyclin partner. Any constituent part of a cell, the basic structural and functional unit of all organisms. The subcomplex of the proteasome regulatory particle that forms the peripheral lid, which is added on top of the base subcomplex. The subcomplex of the proteasome regulatory particle that directly associates with the proteasome core complex. Any protein complex that binds to an mRNA cap at any time in the lifetime of the mRNA. A conserved heterodimeric protein complex that binds to the 5' terminal cap structure m7G(5')ppp(5')N of nascent eukaryotic RNA polymerase II transcripts such as pre-mRNA and U snRNA. The consists of proteins known as CBP20 and CBP80, binds to cap structures in the nucleus, and is involved in pre-mRNA splicing, 3'-end formation, and RNA nuclear export. Heterotrimeric enzyme complex, which in humans is composed of two large subunits of the same size, and one smaller subunit. Functions in the addition of nucleotide-activated sugars onto the polypeptide. An enzyme complex that catalyzes the removal of serine- or threonine-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase. The portion of the plasma membrane surrounding a stereocilium. A multienzyme complex usually composed of four proteins, EntB, EntD, EntE and EntF. Plays a role in the enterobactin biosynthesis pathway. A complex that posseses mannosyltransferase activity. A protein complex that includes a ubiquitin-protein ligase and other proteins that may confer substrate specificity on the complex. A protein complex comprised of members of the ClpX, ClpC, ClpD, ClpP or ClpR protein families. ClpPs are the proteolytic subunit of active complexes, and ClpA and ClpX form the regulatory subunits. Enzymatically active and inactive complexes can form. All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. A homodimeric protein complex that possesses 4-aminobutyrate transaminase activity. Any constituent part of a thylakoid, a sac-like vesicle that bears the photosynthetic pigments in photosynthetic organisms. A multisubunit complex that activates the hydrolysis of small nonubiquitinated peptides by binding to the proteasome core complex. DNA structures that are not part of a chromosome. The intracellular plane, located halfway between the poles of the spindle, where chromosomes align during metaphase of mitotic or meiotic nuclear division. A heterodimeric calcium ion and calmodulin dependent protein phosphatase composed of catalytic and regulatory subunits; the regulatory subunit is very similar in sequence to calmodulin. A protein-pigment complex that may be closely or peripherally associated to photosynthetic reaction centers that participate in harvesting and transferring radiant energy to the reaction center. The lipid bilayer surrounding the platelet dense tubular network. A protein complex that possesses protein serine/threonine kinase activity, and contains two catalytic alpha subunits and two regulatory beta subunits. Protein kinase CK2 complexes are found in nearly every subcellular compartment, and can phosphorylate many protein substrates in addition to casein. A heterodimeric enzyme, composed of an alpha and a beta subunit. Participates in the post-translational C-terminal modification of several small GTPases, allowing their targeting to the membrane. An enzyme complex which in eukaryotes is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Catalyzes the phosphorylation of proteins to O-phosphoproteins. A protein complex that stimulates the exchange of guanyl nucleotides associated with a GTPase. Complex that catalyzes the synthesis of ADP-glucose and pyrophosphate from glucose-1-phosphate and ATP. In plants, the complex is a heterotetramer composed of two types of subunits (small and large). In bacteria, the enzyme complex is composed of four identical subunits. An enzyme complex that catalyzes the breakdown of ethanolamine to form acetaldehyde and ammonia. The complex infective apparatus corresponding to the central mass of cytoplasm within a spore that is injected into a host cell by various parasitic microorganisms. An enzyme complex, composed of regulatory and catalytic subunits, that catalyzes protein phosphorylation. Inactive forms of the enzyme have two regulatory chains and two catalytic chains; activation by cAMP produces two active catalytic monomers and a regulatory dimer. A heterodimeric protein complex that possesses 4-amino-4-deoxychorismate synthase activity. An enzyme complex composed of two proteins, dinitrogenase and nitrogenase reductase; dinitrogenase is tetrameric with an alpha2-beta2 structure and nitrogenase reductase is a homodimer, and both are associated with metal ions, which differ between species. Both proteins are required for the enzyme activity of the complex, the formation of oxidized ferredoxin and ammonia from reduced ferredoxin and nitrogen. A protein complex that plays a role in DNA double-strand break repair via nonhomologous end joining. Such complexes typically contain a specialized DNA ligase (e.g. Lig4 in eukaryotes) and one or more proteins that bind to DNA ends. The proteasome core subcomplex that constitutes the two inner rings of the proteasome core complex. An example of this component is found in Mus musculus. Any constituent part of the cytoplasm, all of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. Circular DNA structures that are not part of a chromosome. The complex formed by the catalytic subunit of protein phosphatase 4 plus a regulatory subunit. The proteasome core subcomplex that constitutes the two outer rings of the proteasome core complex. An example of this component is found in Mus musculus. A heterodimeric protein complex formed of superoxide dismutase 1 and Bcl-2. Complex formation is thought to link superoxide dismutase to an apoptotic pathway. A protein complex that contains the survival motor neuron (SMN) protein and at least eight additional integral components, including the Gemin2-8 and Unrip proteins; the complex is found in the cytoplasm and in nuclear Gems, and is involved in spliceosomal snRNP assembly in the cytoplasm and in pre-mRNA splicing in the nucleus. Any constituent part of an axoneme, the bundle of microtubules and associated proteins that forms the core of cilia and flagella in eukaryotic cells and is responsible for their movements. A macromolecular complex containing both protein and RNA molecules. A constituent part of an intracellular organelle, an organized structure of distinctive morphology and function, occurring within the cell. Includes constituent parts of the nucleus, mitochondria, plastids, vacuoles, vesicles, ribosomes and the cytoskeleton but excludes the plasma membrane. A protein complex that contains Gemin6, Gemin7, and unrip (STRAP), and can bind to snRNAs; may play a role in snRNP assembly. A multisubunit complex that recognizes and unfolds core proteasome substrate proteins, and translocates them to the core complex in an ATP dependent manner. A protein complex that possesses GTP cyclohydrolase I activity. In E. coli and human, the complex is a homodecamer, and monomers are catalytically inactive. A protein complex that contains the survival motor neuron (SMN) protein and Gemin2; may form the stable core of the larger SMN complex. A protein complex, that caps one or both ends of the proteasome core complex and regulates entry into, or exit from, the proteasome core complex. A protein complex that contains Gemin3 (DDX20), Gemin4, and Gemin5, and can bind to snRNAs; may be an intermediate in SMN complex assembly.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: intracellular part
Acc: GO:0044424
Aspect: Cellular Component
Desc: Any constituent part of the living contents of a cell; the matter contained within (but not including) the plasma membrane, usually taken to exclude large vacuoles and masses of secretory or ingested material. In eukaryotes it includes the nucleus and cytoplasm.
Proteins in PDR annotated with:
   This term: 52 [Search]
   Term or descendants: 52551 [Refine Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0044424 - intracellular part (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle