Name | Number of supported studies | Average coverage | |
---|---|---|---|
peripheral blood | 17 studies | 33% ± 12% | |
lung | 15 studies | 38% ± 14% | |
intestine | 10 studies | 31% ± 16% | |
brain | 10 studies | 32% ± 13% | |
kidney | 8 studies | 32% ± 8% | |
eye | 7 studies | 41% ± 16% | |
bone marrow | 5 studies | 25% ± 6% | |
lymph node | 5 studies | 33% ± 13% | |
pancreas | 4 studies | 44% ± 19% | |
placenta | 4 studies | 44% ± 21% | |
uterus | 4 studies | 45% ± 14% | |
liver | 4 studies | 41% ± 29% | |
breast | 4 studies | 31% ± 5% | |
adrenal gland | 3 studies | 30% ± 3% |
Tissue | GTEx Coverage | GTEx Average TPM | GTEx Number of samples | TCGA Coverage | TCGA Average TPM | TCGA Number of samples |
---|---|---|---|---|---|---|
esophagus | 100% | 19736.61 | 1445 / 1445 | 100% | 243.34 | 183 / 183 |
ovary | 100% | 17090.45 | 180 / 180 | 100% | 345.49 | 430 / 430 |
uterus | 100% | 19317.51 | 170 / 170 | 100% | 414.83 | 459 / 459 |
brain | 100% | 23659.39 | 2641 / 2642 | 100% | 334.46 | 705 / 705 |
skin | 100% | 20334.06 | 1808 / 1809 | 100% | 321.15 | 472 / 472 |
thymus | 100% | 14825.93 | 653 / 653 | 100% | 262.51 | 604 / 605 |
stomach | 100% | 12352.20 | 359 / 359 | 100% | 173.34 | 285 / 286 |
kidney | 100% | 16976.93 | 89 / 89 | 100% | 248.63 | 897 / 901 |
breast | 100% | 16044.30 | 459 / 459 | 99% | 272.11 | 1112 / 1118 |
intestine | 100% | 18391.21 | 966 / 966 | 99% | 184.03 | 524 / 527 |
prostate | 100% | 18738.18 | 245 / 245 | 99% | 259.60 | 499 / 502 |
lung | 100% | 17117.01 | 577 / 578 | 99% | 331.48 | 1149 / 1155 |
adrenal gland | 100% | 33645.33 | 258 / 258 | 99% | 292.48 | 228 / 230 |
liver | 100% | 7372.31 | 225 / 226 | 100% | 145.76 | 404 / 406 |
bladder | 100% | 21281.10 | 21 / 21 | 98% | 284.64 | 496 / 504 |
pancreas | 95% | 5440.86 | 312 / 328 | 99% | 239.65 | 177 / 178 |
adipose | 100% | 17953.92 | 1204 / 1204 | 0% | 0 | 0 / 0 |
blood vessel | 100% | 19467.60 | 1335 / 1335 | 0% | 0 | 0 / 0 |
eye | 0% | 0 | 0 / 0 | 100% | 333.51 | 80 / 80 |
lymph node | 0% | 0 | 0 / 0 | 100% | 253.03 | 29 / 29 |
spleen | 100% | 15204.94 | 241 / 241 | 0% | 0 | 0 / 0 |
tonsil | 0% | 0 | 0 / 0 | 100% | 450.75 | 45 / 45 |
ureter | 0% | 0 | 0 / 0 | 100% | 199.87 | 1 / 1 |
peripheral blood | 100% | 12448.23 | 927 / 929 | 0% | 0 | 0 / 0 |
muscle | 99% | 9363.23 | 796 / 803 | 0% | 0 | 0 / 0 |
heart | 99% | 15690.39 | 852 / 861 | 0% | 0 | 0 / 0 |
abdomen | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
bone marrow | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
diaphragm | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
gingiva | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nasal cavity | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nasopharynx | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
nose | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
placenta | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
spinal column | 0% | 0 | 0 / 0 | 0% | 0 | 0 / 0 |
GO_1900244 | Biological process | positive regulation of synaptic vesicle endocytosis |
GO_0031623 | Biological process | receptor internalization |
GO_0098884 | Biological process | postsynaptic neurotransmitter receptor internalization |
GO_0048488 | Biological process | synaptic vesicle endocytosis |
GO_0006886 | Biological process | intracellular protein transport |
GO_0002092 | Biological process | positive regulation of receptor internalization |
GO_0065003 | Biological process | protein-containing complex assembly |
GO_0016192 | Biological process | vesicle-mediated transport |
GO_0006900 | Biological process | vesicle budding from membrane |
GO_0072583 | Biological process | clathrin-dependent endocytosis |
GO_0097494 | Biological process | regulation of vesicle size |
GO_1903077 | Biological process | negative regulation of protein localization to plasma membrane |
GO_0098978 | Cellular component | glutamatergic synapse |
GO_0005886 | Cellular component | plasma membrane |
GO_0031410 | Cellular component | cytoplasmic vesicle |
GO_0030122 | Cellular component | AP-2 adaptor complex |
GO_0030666 | Cellular component | endocytic vesicle membrane |
GO_0009898 | Cellular component | cytoplasmic side of plasma membrane |
GO_0070062 | Cellular component | extracellular exosome |
GO_0030669 | Cellular component | clathrin-coated endocytic vesicle membrane |
GO_0098794 | Cellular component | postsynapse |
GO_0098894 | Cellular component | extrinsic component of presynaptic endocytic zone membrane |
GO_0005829 | Cellular component | cytosol |
GO_0045334 | Cellular component | clathrin-coated endocytic vesicle |
GO_0005905 | Cellular component | clathrin-coated pit |
GO_0005765 | Cellular component | lysosomal membrane |
GO_0036020 | Cellular component | endolysosome membrane |
GO_0008289 | Molecular function | lipid binding |
GO_0005048 | Molecular function | signal sequence binding |
GO_0050750 | Molecular function | low-density lipoprotein particle receptor binding |
GO_0035615 | Molecular function | clathrin adaptor activity |
GO_0044325 | Molecular function | transmembrane transporter binding |
GO_0097718 | Molecular function | disordered domain specific binding |
GO_0005515 | Molecular function | protein binding |
Gene name | AP2M1 |
Protein name | AP-2 complex subunit mu (AP-2 mu chain) (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat assembly protein AP50) (Clathrin coat-associated protein AP50) (Plasma membrane adaptor AP-2 50 kDa protein) Adaptor related protein complex 2 subunit mu 1 AP-2 complex subunit mu (AP-2 mu chain) (Adaptin-mu2) (Adaptor protein complex AP-2 subunit mu) (Adaptor-related protein complex 2 subunit mu) (Clathrin assembly protein complex 2 mu medium chain) (Clathrin coat assembly protein AP50) (Clathrin coat-associated protein AP50) (HA2 50 kDa subunit) (Plasma membrane adaptor AP-2 50 kDa protein) AP-2 complex subunit mu |
Synonyms | KIAA0109 CLAPM1 |
Description | FUNCTION: Component of the adaptor protein complex 2 (AP-2) . Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways . Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation . AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome . The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components . Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation . AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis . AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface . AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules (By similarity). AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway . During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 . The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs (By similarity). The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at Thr-156 in membrane-associated AP-2 . The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 . Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity). . FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. . FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. . FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. . FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. . FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. . FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. . FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. . |
Accessions | A0A087WY71 ENST00000686364.1 ENST00000690285.1 C9JGT8 C9JJ47 C9JJD3 ENST00000621863.5 [Q96CW1-2] ENST00000455925.2 C9JTK4 H7C4C3 ENST00000439647.5 [Q96CW1-2] ENST00000431779.6 ENST00000688579.1 ENST00000686942.1 A0A8I5KTP2 ENST00000442686.2 ENST00000427072.6 A0A8I5KWD3 E9PFW3 ENST00000621863 ENST00000432591.6 ENST00000411763.6 ENST00000292807.9 [Q96CW1-1] A0A8I5QJU5 Q96CW1 ENST00000448139.6 C9JPV8 A0A8I5KT55 ENST00000382456.7 [Q96CW1-2] |