| UniProt ID | AT1B3_HUMAN | |
|---|---|---|
| UniProt AC | P54709 | |
| Protein Name | Sodium/potassium-transporting ATPase subunit beta-3 | |
| Gene Name | ATP1B3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 279 | |
| Subcellular Localization |
Cell membrane Single-pass type II membrane protein . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV. |
|
| Protein Description | This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known.. | |
| Protein Sequence | MTKNEKKSLNQSLAEWKLFIYNPTTGEFLGRTAKSWGLILLFYLVFYGFLAALFSFTMWVMLQTLNDEVPKYRDQIPSPGLMVFPKPVTALEYTFSRSDPTSYAGYIEDLKKFLKPYTLEEQKNLTVCPDGALFEQKGPVYVACQFPISLLQACSGMNDPDFGYSQGNPCILVKMNRIIGLKPEGVPRIDCVSKNEDIPNVAVYPHNGMIDLKYFPYYGKKLHVGYLQPLVAVQVSFAPNNTGKEVTVECKIDGSANLKSQDDRDKFLGRVMFKITARA | |
| 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 |
|---|---|---|---|---|---|
| 3 | Ubiquitination | -----MTKNEKKSLN -----CCHHHHHHHH | 62.91 | 23000965 | |
| 6 | Ubiquitination | --MTKNEKKSLNQSL --CCHHHHHHHHHHH | 57.99 | 23000965 | |
| 7 | Ubiquitination | -MTKNEKKSLNQSLA -CCHHHHHHHHHHHH | 54.73 | 23000965 | |
| 8 | Phosphorylation | MTKNEKKSLNQSLAE CCHHHHHHHHHHHHH | 43.55 | 28188228 | |
| 12 | Phosphorylation | EKKSLNQSLAEWKLF HHHHHHHHHHHEEEE | 28.59 | 25159151 | |
| 17 | Ubiquitination | NQSLAEWKLFIYNPT HHHHHHEEEEEECCC | 25.65 | 21906983 | |
| 72 | Ubiquitination | LNDEVPKYRDQIPSP HCCCCCHHHHCCCCC | 17.22 | - | |
| 86 | Ubiquitination | PGLMVFPKPVTALEY CCEEEECCCEEEEEE | 40.43 | 21963094 | |
| 97 | Ubiquitination | ALEYTFSRSDPTSYA EEEEEEECCCCCCCH | 40.67 | 21906983 | |
| 98 | Ubiquitination | LEYTFSRSDPTSYAG EEEEEECCCCCCCHH | 46.90 | - | |
| 98 | Phosphorylation | LEYTFSRSDPTSYAG EEEEEECCCCCCCHH | 46.90 | 28152594 | |
| 101 | Phosphorylation | TFSRSDPTSYAGYIE EEECCCCCCCHHHHH | 39.08 | 28152594 | |
| 101 | Ubiquitination | TFSRSDPTSYAGYIE EEECCCCCCCHHHHH | 39.08 | 21906983 | |
| 102 | Phosphorylation | FSRSDPTSYAGYIED EECCCCCCCHHHHHH | 20.55 | 28152594 | |
| 103 | Phosphorylation | SRSDPTSYAGYIEDL ECCCCCCCHHHHHHH | 13.41 | 28152594 | |
| 106 | Phosphorylation | DPTSYAGYIEDLKKF CCCCCHHHHHHHHHH | 7.93 | 28152594 | |
| 109 | Ubiquitination | SYAGYIEDLKKFLKP CCHHHHHHHHHHHCC | 54.98 | - | |
| 111 | Acetylation | AGYIEDLKKFLKPYT HHHHHHHHHHHCCCC | 54.52 | 26051181 | |
| 111 | Ubiquitination | AGYIEDLKKFLKPYT HHHHHHHHHHHCCCC | 54.52 | 21906983 | |
| 112 | Ubiquitination | GYIEDLKKFLKPYTL HHHHHHHHHHCCCCH | 64.33 | 21963094 | |
| 112 | Acetylation | GYIEDLKKFLKPYTL HHHHHHHHHHCCCCH | 64.33 | 7851841 | |
| 115 | Ubiquitination | EDLKKFLKPYTLEEQ HHHHHHHCCCCHHHH | 38.83 | 21906983 | |
| 123 | Ubiquitination | PYTLEEQKNLTVCPD CCCHHHHCCCEECCC | 58.15 | 29967540 | |
| 124 | N-linked_Glycosylation | YTLEEQKNLTVCPDG CCHHHHCCCEECCCC | 40.41 | 17660510 | |
| 137 | Ubiquitination | DGALFEQKGPVYVAC CCHHHCCCCCEEEEE | 58.97 | 29967540 | |
| 160 | Ubiquitination | ACSGMNDPDFGYSQG HHCCCCCCCCCCCCC | 33.55 | - | |
| 168 | Ubiquitination | DFGYSQGNPCILVKM CCCCCCCCEEEEEEC | 22.19 | 21906983 | |
| 174 | Ubiquitination | GNPCILVKMNRIIGL CCEEEEEECCCCCCC | 27.32 | 21963094 | |
| 182 | Acetylation | MNRIIGLKPEGVPRI CCCCCCCCCCCCCCE | 35.49 | 26051181 | |
| 182 | Ubiquitination | MNRIIGLKPEGVPRI CCCCCCCCCCCCCCE | 35.49 | 21906983 | |
| 194 | Acetylation | PRIDCVSKNEDIPNV CCEECEECCCCCCCE | 43.91 | 26051181 | |
| 194 | Ubiquitination | PRIDCVSKNEDIPNV CCEECEECCCCCCCE | 43.91 | 21963094 | |
| 213 | Ubiquitination | HNGMIDLKYFPYYGK CCCEEEEEEECCCCC | 40.89 | 21906983 | |
| 220 | 2-Hydroxyisobutyrylation | KYFPYYGKKLHVGYL EEECCCCCEEEEECC | 35.72 | - | |
| 220 | Ubiquitination | KYFPYYGKKLHVGYL EEECCCCCEEEEECC | 35.72 | 21963094 | |
| 221 | Ubiquitination | YFPYYGKKLHVGYLQ EECCCCCEEEEECCC | 39.19 | 22817900 | |
| 240 | N-linked_Glycosylation | VQVSFAPNNTGKEVT EEEEECCCCCCCEEE | 56.09 | 12754519 | |
| 240 | N-linked_Glycosylation | VQVSFAPNNTGKEVT EEEEECCCCCCCEEE | 56.09 | 12754519 | |
| 241 | N-linked_Glycosylation | QVSFAPNNTGKEVTV EEEECCCCCCCEEEE | 49.50 | - | |
| 241 | N-linked_Glycosylation | QVSFAPNNTGKEVTV EEEECCCCCCCEEEE | 49.50 | 19349973 | |
| 251 | Ubiquitination | KEVTVECKIDGSANL CEEEEEEEECCCCCC | 30.26 | 29967540 | |
| 259 | Ubiquitination | IDGSANLKSQDDRDK ECCCCCCCCHHHHHH | 45.97 | 21906983 | |
| 266 | Ubiquitination | KSQDDRDKFLGRVMF CCHHHHHHHHHHHHH | 43.30 | 29967540 | |
| 274 | Ubiquitination | FLGRVMFKITARA-- HHHHHHHEEEECC-- | 22.50 | 29967540 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of AT1B3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AT1B3_HUMAN !! | ||||||
* 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 AT1B3_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| D00112 | G-Strophanthin (JAN); Ouabain; Ouabain octahydrate | |||||
| D00297 | Digitoxin (JP16/USP/INN); Crystodigin (TN) | |||||
| D00298 | Digoxin (JP16/USP); Lanoxicaps (TN); Lanoxin (TN) | |||||
| D01240 | Deslanoside (JP16/USP/INN); Cedilanid-d (TN) | |||||
| D01379 | Proscillaridin (JAN/USAN/INN); Talusin (TN) | |||||
| D01972 | Lanatoside C (JP16/INN); Digilanogen C (TN) | |||||
| D02587 | Metildigoxin (JP16); Lanirapid (TN) | |||||
| D06881 | Acetyldigitoxin (INN); Acylanid (TN) | |||||
| D07147 | Gitoformate (INN) | |||||
| D07555 | Acetyldigoxin; Cedigossima (TN) | |||||
| D07556 | beta-Acetyldigoxin; Acetyldigoxin beta isomer; Corotal (TN) | |||||
| D09847 | Metildigoxin (INN); Medigoxin (BAN) | |||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-240. | |