AT1B1_HUMAN - dbPTM
AT1B1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AT1B1_HUMAN
UniProt AC P05026
Protein Name Sodium/potassium-transporting ATPase subunit beta-1
Gene Name ATP1B1
Organism Homo sapiens (Human).
Sequence Length 303
Subcellular Localization Cell membrane
Single-pass type II membrane protein . Cell membrane, sarcolemma . Colocalizes with OBSCN at the intercalated disk and sarcolemma in cardiomyocytes. Localizes in long striations at the level of Z and M lines.
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 beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane.; Involved in cell adhesion and establishing epithelial cell polarity..
Protein Sequence MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLNDETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKVGNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
11PhosphorylationGKAKEEGSWKKFIWN
CCCCCCCCCCCEEEE		38.7128348404
132-HydroxyisobutyrylationAKEEGSWKKFIWNSE
CCCCCCCCCEEEECH		39.23-
13UbiquitinationAKEEGSWKKFIWNSE
CCCCCCCCCEEEECH		39.23-
14UbiquitinationKEEGSWKKFIWNSEK
CCCCCCCCEEEECHH		35.50-
21UbiquitinationKFIWNSEKKEFLGRT
CEEEECHHHHHHCCC		58.38-
85UbiquitinationTQIPQIQKTEISFRP
CCCCCCEEEEEEECC		50.16-
96UbiquitinationSFRPNDPKSYEAYVL
EECCCCCCHHHHHHH		69.41-
96 (in isoform 2)Ubiquitination-69.41-
97PhosphorylationFRPNDPKSYEAYVLN
ECCCCCCHHHHHHHH		33.3328152594
98PhosphorylationRPNDPKSYEAYVLNI
CCCCCCHHHHHHHHH		15.6528152594
101PhosphorylationDPKSYEAYVLNIVRF
CCCHHHHHHHHHHHH		8.1122817900
1132-HydroxyisobutyrylationVRFLEKYKDSAQRDD
HHHHHHHHHHHCCCC		57.16-
113UbiquitinationVRFLEKYKDSAQRDD
HHHHHHHHHHHCCCC		57.16-
118MethylationKYKDSAQRDDMIFED
HHHHHHCCCCCEEEC		41.43-
118DimethylationKYKDSAQRDDMIFED
HHHHHHCCCCCEEEC		41.43-
121SulfoxidationDSAQRDDMIFEDCGD
HHHCCCCCEEECCCC		4.4128465586
134UbiquitinationGDVPSEPKERGDFNH
CCCCCCCHHCCCCCC		56.86-
147UbiquitinationNHERGERKVCRFKLE
CCCCCCCEEEEEEEE		41.19-
152UbiquitinationERKVCRFKLEWLGNC
CCEEEEEEEEECCCC		26.58-
158N-linked_GlycosylationFKLEWLGNCSGLNDE
EEEEECCCCCCCCCC		18.0112754519
170UbiquitinationNDETYGYKEGKPCII
CCCCCCCCCCCEEEE		56.48-
173UbiquitinationTYGYKEGKPCIIIKL
CCCCCCCCEEEEEEE		37.50-
179UbiquitinationGKPCIIIKLNRVLGF
CCEEEEEEECCCCCC		29.33-
187UbiquitinationLNRVLGFKPKPPKNE
ECCCCCCCCCCCCCC		50.78-
193N-linked_GlycosylationFKPKPPKNESLETYP
CCCCCCCCCCCCCCC		50.2712754519
195PhosphorylationPKPPKNESLETYPVM
CCCCCCCCCCCCCEE		40.6830242111
198PhosphorylationPKNESLETYPVMKYN
CCCCCCCCCCEEECC		38.1230242111
199PhosphorylationKNESLETYPVMKYNP
CCCCCCCCCEEECCC		5.6230242111
216UbiquitinationLPVQCTGKRDEDKDK
ECEECCCCCCCCCCC		38.22-
2162-HydroxyisobutyrylationLPVQCTGKRDEDKDK
ECEECCCCCCCCCCC		38.22-
221UbiquitinationTGKRDEDKDKVGNVE
CCCCCCCCCCCCCEE		58.35-
223UbiquitinationKRDEDKDKVGNVEYF
CCCCCCCCCCCEEEE		58.75-
229PhosphorylationDKVGNVEYFGLGNSP
CCCCCEEEEECCCCC		9.9229978859
235PhosphorylationEYFGLGNSPGFPLQY
EEEECCCCCCCCCHH		25.3029978859
242PhosphorylationSPGFPLQYYPYYGKL
CCCCCCHHHCCCCEE		17.6829978859
243PhosphorylationPGFPLQYYPYYGKLL
CCCCCHHHCCCCEEC		3.3329978859
245PhosphorylationFPLQYYPYYGKLLQP
CCCHHHCCCCEECCH		14.5529978859
246PhosphorylationPLQYYPYYGKLLQPK
CCHHHCCCCEECCHH		11.8629978859
248 (in isoform 2)Ubiquitination-29.87-
248UbiquitinationQYYPYYGKLLQPKYL
HHHCCCCEECCHHHH		29.87-
254PhosphorylationGKLLQPKYLQPLLAV
CEECCHHHHHHEEEE		19.77-
265N-linked_GlycosylationLLAVQFTNLTMDTEI
EEEEEEECCCCCCEE		34.5012754519
265N-linked_GlycosylationLLAVQFTNLTMDTEI
EEEEEEECCCCCCEE		34.5019522481
277UbiquitinationTEIRIECKAYGENIG
CEEEEEEEECCCCCC		31.67-
285PhosphorylationAYGENIGYSEKDRFQ
ECCCCCCCCHHHCCC		15.17-
288UbiquitinationENIGYSEKDRFQGRF
CCCCCCHHHCCCCEE		48.54-
2882-HydroxyisobutyrylationENIGYSEKDRFQGRF
CCCCCCHHHCCCCEE		48.54-
288AcetylationENIGYSEKDRFQGRF
CCCCCCHHHCCCCEE		48.5427452117
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseRNF183Q96D59
PMID:31732153
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AT1B1_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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 AT1B1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLM_HUMANFXYD1physical
14597563
LRIF1_HUMANLRIF1physical
16169070
NDRG2_HUMANNDRG2physical
21771789
KMT2B_HUMANKMT2Bphysical
21900206
TRM2A_HUMANTRMT2Aphysical
21900206
DDAH2_HUMANDDAH2physical
21900206
PSME1_HUMANPSME1physical
21900206
CRIP2_HUMANCRIP2physical
21900206
EZH2_HUMANEZH2physical
21900206
THIM_HUMANACAA2physical
26344197
THIL_HUMANACAT1physical
26344197
AT1A1_HUMANATP1A1physical
26344197
AT2A2_HUMANATP2A2physical
26344197
AT5F1_HUMANATP5F1physical
26344197
ATP5L_HUMANATP5Lphysical
26344197
CALX_HUMANCANXphysical
26344197
CX6B1_HUMANCOX6B1physical
26344197
CPT2_HUMANCPT2physical
26344197
CATD_HUMANCTSDphysical
26344197
CY1_HUMANCYC1physical
26344197
ODP2_HUMANDLATphysical
26344197
IF4H_HUMANEIF4Hphysical
26344197
FUBP1_HUMANFUBP1physical
26344197
DHB12_HUMANHSD17B12physical
26344197
MTCH1_HUMANMTCH1physical
26344197
MTCH2_HUMANMTCH2physical
26344197
NDUAC_HUMANNDUFA12physical
26344197
NDUA2_HUMANNDUFA2physical
26344197
NDUS1_HUMANNDUFS1physical
26344197
NDUS3_HUMANNDUFS3physical
26344197
NDUV1_HUMANNDUFV1physical
26344197
PSMD6_HUMANPSMD6physical
26344197
RAB1B_HUMANRAB1Bphysical
26344197
RL26_HUMANRPL26physical
26344197
RS19_HUMANRPS19physical
26344197
TOM40_HUMANTOMM40physical
26344197
QCR7_HUMANUQCRBphysical
26344197
UCRI_HUMANUQCRFS1physical
26344197
QCR8_HUMANUQCRQphysical
26344197
VDAC1_HUMANVDAC1physical
26344197
Drug and Disease Associations
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.
Regulatory Network of AT1B1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158; ASN-193 AND ASN-265,AND MASS SPECTROMETRY.
"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-158; ASN-193 AND ASN-265.

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