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 | ||
* 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. |