| UniProt ID | AP2M1_HUMAN | |
|---|---|---|
| UniProt AC | Q96CW1 | |
| Protein Name | AP-2 complex subunit mu | |
| Gene Name | AP2M1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 435 | |
| Subcellular Localization |
Cell membrane. Membrane, coated pit Peripheral membrane protein Cytoplasmic side. AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.. |
|
| Protein Description | 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. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. 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 'Tyr-156' in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity).. | |
| Protein Sequence | MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKRSNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGYPQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRC | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 45 | Phosphorylation | HARQQVRSPVTNIAR CHHHHHCCCCCCHHC | 25.51 | 21082442 | |
| 59 | 2-Hydroxyisobutyrylation | RTSFFHVKRSNIWLA CEEEEEEECCCEEEE | 41.35 | - | |
| 134 | Phosphorylation | GALKTFITQQGIKSQ CHHHHHHHHHHHHHC | 15.62 | - | |
| 139 | Ubiquitination | FITQQGIKSQHQTKE HHHHHHHHHCCCCHH | 51.38 | 21906983 | |
| 139 (in isoform 1) | Ubiquitination | - | 51.38 | 21890473 | |
| 140 | Phosphorylation | ITQQGIKSQHQTKEE HHHHHHHHCCCCHHH | 30.86 | 27080861 | |
| 144 | Phosphorylation | GIKSQHQTKEEQSQI HHHHCCCCHHHHHHH | 37.99 | 27080861 | |
| 147 (in isoform 2) | Phosphorylation | - | 58.02 | 29507054 | |
| 149 | Phosphorylation | HQTKEEQSQITSQVT CCCHHHHHHHHHHHH | 27.16 | 23403867 | |
| 150 (in isoform 2) | Phosphorylation | - | 42.55 | 29507054 | |
| 151 (in isoform 2) | Phosphorylation | - | 4.91 | 29116813 | |
| 152 | Phosphorylation | KEEQSQITSQVTGQI HHHHHHHHHHHHHCC | 12.89 | 24300666 | |
| 153 | Phosphorylation | EEQSQITSQVTGQIG HHHHHHHHHHHHCCC | 25.04 | 23898821 | |
| 154 | Phosphorylation | EQSQITSQVTGQIGW HHHHHHHHHHHCCCC | 28.30 | - | |
| 154 (in isoform 2) | Phosphorylation | - | 28.30 | 25849741 | |
| 156 | Phosphorylation | SQITSQVTGQIGWRR HHHHHHHHHCCCCCC | 18.74 | 19664994 | |
| 203 | Acetylation | VSGRVVMKSYLSGMP ECCCHHHHHHHCCCC | 25.08 | 30586955 | |
| 209 | Sulfoxidation | MKSYLSGMPECKFGM HHHHHCCCCCCCCCC | 1.96 | 30846556 | |
| 212 | S-nitrosylation | YLSGMPECKFGMNDK HHCCCCCCCCCCCCE | 3.49 | 2212679 | |
| 213 | Acetylation | LSGMPECKFGMNDKI HCCCCCCCCCCCCEE | 43.20 | 26051181 | |
| 217 | Ubiquitination | PECKFGMNDKIVIEK CCCCCCCCCEEEEEE | 48.04 | - | |
| 219 | Acetylation | CKFGMNDKIVIEKQG CCCCCCCEEEEEECC | 33.59 | 25953088 | |
| 222 | Ubiquitination | GMNDKIVIEKQGKGT CCCCEEEEEECCCCC | 6.61 | - | |
| 222 (in isoform 2) | Ubiquitination | - | 6.61 | 21890473 | |
| 224 | Acetylation | NDKIVIEKQGKGTAD CCEEEEEECCCCCCC | 53.91 | 25953088 | |
| 224 | Ubiquitination | NDKIVIEKQGKGTAD CCEEEEEECCCCCCC | 53.91 | 21906983 | |
| 224 (in isoform 1) | Ubiquitination | - | 53.91 | 21890473 | |
| 225 | Ubiquitination | DKIVIEKQGKGTADE CEEEEEECCCCCCCC | 46.14 | - | |
| 225 (in isoform 2) | Ubiquitination | - | 46.14 | 21890473 | |
| 227 | Ubiquitination | IVIEKQGKGTADETS EEEEECCCCCCCCCC | 51.06 | 21906983 | |
| 227 (in isoform 1) | Ubiquitination | - | 51.06 | 21890473 | |
| 229 | Phosphorylation | IEKQGKGTADETSKS EEECCCCCCCCCCCC | 34.13 | 28857561 | |
| 233 | Phosphorylation | GKGTADETSKSGKQS CCCCCCCCCCCCCCE | 41.84 | 28857561 | |
| 233 | Ubiquitination | GKGTADETSKSGKQS CCCCCCCCCCCCCCE | 41.84 | - | |
| 233 (in isoform 2) | Ubiquitination | - | 41.84 | 21890473 | |
| 234 | Phosphorylation | KGTADETSKSGKQSI CCCCCCCCCCCCCEE | 23.83 | 18691976 | |
| 235 | Ubiquitination | GTADETSKSGKQSIA CCCCCCCCCCCCEEE | 71.32 | 21906983 | |
| 235 (in isoform 1) | Ubiquitination | - | 71.32 | 21890473 | |
| 236 | Phosphorylation | TADETSKSGKQSIAI CCCCCCCCCCCEEEE | 51.49 | 18691976 | |
| 236 | Ubiquitination | TADETSKSGKQSIAI CCCCCCCCCCCEEEE | 51.49 | - | |
| 238 | Malonylation | DETSKSGKQSIAIDD CCCCCCCCCEEEEEC | 48.22 | 26320211 | |
| 238 | Phosphorylation | DETSKSGKQSIAIDD CCCCCCCCCEEEEEC | 48.22 | - | |
| 238 | Ubiquitination | DETSKSGKQSIAIDD CCCCCCCCCEEEEEC | 48.22 | - | |
| 240 | Phosphorylation | TSKSGKQSIAIDDCT CCCCCCCEEEEECCC | 19.92 | 28857561 | |
| 247 | Phosphorylation | SIAIDDCTFHQCVRL EEEEECCCHHHEEEH | 31.01 | 25002506 | |
| 254 | Acetylation | TFHQCVRLSKFDSER CHHHEEEHHHCCCCC | 3.05 | - | |
| 254 | Ubiquitination | TFHQCVRLSKFDSER CHHHEEEHHHCCCCC | 3.05 | - | |
| 254 (in isoform 2) | Ubiquitination | - | 3.05 | 21890473 | |
| 256 | Acetylation | HQCVRLSKFDSERSI HHEEEHHHCCCCCCE | 58.75 | 25825284 | |
| 256 | Malonylation | HQCVRLSKFDSERSI HHEEEHHHCCCCCCE | 58.75 | 26320211 | |
| 256 | Ubiquitination | HQCVRLSKFDSERSI HHEEEHHHCCCCCCE | 58.75 | - | |
| 256 (in isoform 1) | Ubiquitination | - | 58.75 | 21890473 | |
| 259 | Phosphorylation | VRLSKFDSERSISFI EEHHHCCCCCCEEEC | 37.73 | 10409839 | |
| 262 | Phosphorylation | SKFDSERSISFIPPD HHCCCCCCEEECCCC | 20.66 | 10409851 | |
| 279 | Ubiquitination | FELMRYRTTKDIILP EEEEEEEECCCEEEE | 29.30 | - | |
| 279 (in isoform 2) | Ubiquitination | - | 29.30 | 21890473 | |
| 281 | 2-Hydroxyisobutyrylation | LMRYRTTKDIILPFR EEEEEECCCEEEECC | 46.44 | - | |
| 281 | Malonylation | LMRYRTTKDIILPFR EEEEEECCCEEEECC | 46.44 | 26320211 | |
| 281 | Ubiquitination | LMRYRTTKDIILPFR EEEEEECCCEEEECC | 46.44 | - | |
| 281 (in isoform 1) | Ubiquitination | - | 46.44 | 21890473 | |
| 302 | Ubiquitination | EVGRTKLEVKVVIKS HHCCCEEEEEEEEEC | 41.68 | - | |
| 304 | Acetylation | GRTKLEVKVVIKSNF CCCEEEEEEEEECCC | 22.78 | 7380767 | |
| 306 | Ubiquitination | TKLEVKVVIKSNFKP CEEEEEEEEECCCCH | 3.65 | - | |
| 308 | Acetylation | LEVKVVIKSNFKPSL EEEEEEEECCCCHHH | 27.95 | 7380779 | |
| 310 | Ubiquitination | VKVVIKSNFKPSLLA EEEEEECCCCHHHEE | 43.91 | - | |
| 310 (in isoform 2) | Ubiquitination | - | 43.91 | 21890473 | |
| 312 | Acetylation | VVIKSNFKPSLLAQK EEEECCCCHHHEEEE | 37.64 | 25953088 | |
| 312 | Malonylation | VVIKSNFKPSLLAQK EEEECCCCHHHEEEE | 37.64 | 26320211 | |
| 312 | Ubiquitination | VVIKSNFKPSLLAQK EEEECCCCHHHEEEE | 37.64 | - | |
| 312 (in isoform 1) | Ubiquitination | - | 37.64 | 21890473 | |
| 319 | Acetylation | KPSLLAQKIEVRIPT CHHHEEEEEEEECCC | 34.92 | 25953088 | |
| 319 | Malonylation | KPSLLAQKIEVRIPT CHHHEEEEEEEECCC | 34.92 | 26320211 | |
| 338 | Sulfoxidation | SGVQVICMKGKAKYK CCCEEEEECCCEEEE | 4.39 | 21406390 | |
| 339 | Acetylation | GVQVICMKGKAKYKA CCEEEEECCCEEEEC | 53.50 | 25953088 | |
| 339 | Ubiquitination | GVQVICMKGKAKYKA CCEEEEECCCEEEEC | 53.50 | - | |
| 343 | Ubiquitination | ICMKGKAKYKASENA EEECCCEEEECCCCC | 51.25 | - | |
| 344 | Phosphorylation | CMKGKAKYKASENAI EECCCEEEECCCCCH | 19.35 | 21709141 | |
| 345 | Malonylation | MKGKAKYKASENAIV ECCCEEEECCCCCHH | 44.74 | 26320211 | |
| 345 | Phosphorylation | MKGKAKYKASENAIV ECCCEEEECCCCCHH | 44.74 | - | |
| 345 | Ubiquitination | MKGKAKYKASENAIV ECCCEEEECCCCCHH | 44.74 | - | |
| 347 | Phosphorylation | GKAKYKASENAIVWK CCEEEECCCCCHHHH | 27.51 | 9424921 | |
| 354 | 2-Hydroxyisobutyrylation | SENAIVWKIKRMAGM CCCCHHHHHHHHHCC | 27.70 | - | |
| 354 | Acetylation | SENAIVWKIKRMAGM CCCCHHHHHHHHHCC | 27.70 | 25953088 | |
| 375 | Phosphorylation | AEIELLPTNDKKKWA EEEEECCCCCCCCCC | 56.89 | 20068231 | |
| 376 | Ubiquitination | EIELLPTNDKKKWAR EEEECCCCCCCCCCC | 58.10 | - | |
| 376 (in isoform 2) | Ubiquitination | - | 58.10 | 21890473 | |
| 378 | Ubiquitination | ELLPTNDKKKWARPP EECCCCCCCCCCCCC | 59.32 | 21906983 | |
| 378 (in isoform 1) | Ubiquitination | - | 59.32 | 21890473 | |
| 378 (in isoform 2) | Ubiquitination | - | 59.32 | 21890473 | |
| 379 | Ubiquitination | LLPTNDKKKWARPPI ECCCCCCCCCCCCCE | 57.31 | - | |
| 380 | Ubiquitination | LPTNDKKKWARPPIS CCCCCCCCCCCCCEE | 52.40 | 21890473 | |
| 380 (in isoform 1) | Ubiquitination | - | 52.40 | 21890473 | |
| 385 | Phosphorylation | KKKWARPPISMNFEV CCCCCCCCEEECEEE | 26.23 | - | |
| 387 | Phosphorylation | KWARPPISMNFEVPF CCCCCCEEECEEECC | 17.28 | 166220859 | |
| 395 | Phosphorylation | MNFEVPFAPSGLKVR ECEEECCCCCCCEEE | 7.41 | - | |
| 397 | Phosphorylation | FEVPFAPSGLKVRYL EEECCCCCCCEEEEE | 54.02 | 166220867 | |
| 398 | Ubiquitination | EVPFAPSGLKVRYLK EECCCCCCCEEEEEE | 28.58 | - | |
| 403 | Phosphorylation | PSGLKVRYLKVFEPK CCCCEEEEEEEECCC | 17.54 | 28152594 | |
| 403 | Ubiquitination | PSGLKVRYLKVFEPK CCCCEEEEEEEECCC | 17.54 | - | |
| 405 | Acetylation | GLKVRYLKVFEPKLN CCEEEEEEEECCCCC | 35.62 | 25953088 | |
| 405 | Malonylation | GLKVRYLKVFEPKLN CCEEEEEEEECCCCC | 35.62 | 26320211 | |
| 405 | Ubiquitination | GLKVRYLKVFEPKLN CCEEEEEEEECCCCC | 35.62 | - | |
| 408 | Ubiquitination | VRYLKVFEPKLNYSD EEEEEEECCCCCCCC | 44.50 | - | |
| 408 (in isoform 2) | Ubiquitination | - | 44.50 | 21890473 | |
| 410 | Acetylation | YLKVFEPKLNYSDHD EEEEECCCCCCCCHH | 42.01 | 25953088 | |
| 410 | Ubiquitination | YLKVFEPKLNYSDHD EEEEECCCCCCCCHH | 42.01 | 21890473 | |
| 410 (in isoform 1) | Ubiquitination | - | 42.01 | 21890473 | |
| 412 | Phosphorylation | KVFEPKLNYSDHDVI EEECCCCCCCCHHHH | 40.15 | - | |
| 413 | Phosphorylation | VFEPKLNYSDHDVIK EECCCCCCCCHHHHH | 26.38 | 28152594 | |
| 414 | Phosphorylation | FEPKLNYSDHDVIKW ECCCCCCCCHHHHHH | 27.65 | 110756115 | |
| 418 | Acetylation | LNYSDHDVIKWVRYI CCCCCHHHHHHHHHH | 4.32 | - | |
| 418 | Ubiquitination | LNYSDHDVIKWVRYI CCCCCHHHHHHHHHH | 4.32 | - | |
| 418 (in isoform 2) | Ubiquitination | - | 4.32 | 21890473 | |
| 420 | 2-Hydroxyisobutyrylation | YSDHDVIKWVRYIGR CCCHHHHHHHHHHCC | 39.21 | - | |
| 420 | Acetylation | YSDHDVIKWVRYIGR CCCHHHHHHHHHHCC | 39.21 | 25825284 | |
| 420 | Ubiquitination | YSDHDVIKWVRYIGR CCCHHHHHHHHHHCC | 39.21 | 2189047 | |
| 420 (in isoform 1) | Ubiquitination | - | 39.21 | 21890473 | |
| 429 | Phosphorylation | VRYIGRSGIYETRC- HHHHCCCCCEECCC- | 25.74 | - | |
| 431 | Phosphorylation | YIGRSGIYETRC--- HHCCCCCEECCC--- | 18.12 | 19835603 | |
| 433 | Phosphorylation | GRSGIYETRC----- CCCCCEECCC----- | 21.99 | 19835603 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 156 | T | Phosphorylation | Kinase | AAK1 | Q2M2I8 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 156 | T | Phosphorylation |
| 11877457 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of AP2M1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND THR-156, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156, AND MASSSPECTROMETRY. | |
