dbPTM

AT1B1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AT1B1_MOUSE
UniProt AC	P14094
Protein Name	Sodium/potassium-transporting ATPase subunit beta-1
Gene Name	Atp1b1
Organism	Mus musculus (Mouse).
Sequence Length	304
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	MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISELKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIIRFLEKYKDSAQKDDMIFEDCGNVPSEPKERGDINHERGERKVCRFKLDWLGNCSGLNDDSYGYREGKPCIIIKLNRVLGFKPKPPKNESLETYPLMMKYNPNVLPVQCTGKRDEDKDKVGNIEYFGMGGYYGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTVDTEIRVECKAYGENIGYSEKDRFQGRFDVKIEIKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	GKAKEEGSWKKFIWN CCCCCCCCCCCEEEE	38.71	22324799
13	Acetylation	AKEEGSWKKFIWNSE CCCCCCCCCEEEECH	39.23	19846943
14	Ubiquitination	KEEGSWKKFIWNSEK CCCCCCCCEEEECHH	35.50	22790023
19	Phosphorylation	WKKFIWNSEKKEFLG CCCEEEECHHHHHHC	35.48	22324799
21	Ubiquitination	KFIWNSEKKEFLGRT CEEEECHHHHHHCCC	58.38	22790023
45	Glutathionylation	FYVIFYGCLAGIFIG HHHHHHHHHHHHHHH	1.28	22833525
101	Phosphorylation	DPKSYEAYVLNIIRF CCHHHHHHHHHHHHH	8.11	22817900
131	Phosphorylation	EDCGNVPSEPKERGD ECCCCCCCCCHHCCC	63.35	25195567
158	N-linked_Glycosylation	FKLDWLGNCSGLNDD EECEECCCCCCCCCC	18.01	19349973
163	N-linked_Glycosylation	LGNCSGLNDDSYGYR CCCCCCCCCCCCCCC	55.35	19349973
193	N-linked_Glycosylation	FKPKPPKNESLETYP CCCCCCCCCCCCCCC	50.27	-
205	Nitration	TYPLMMKYNPNVLPV CCCEEEECCCCCCCE	20.25	-
205	Phosphorylation	TYPLMMKYNPNVLPV CCCEEEECCCCCCCE	20.25	25195567
214	S-palmitoylation	PNVLPVQCTGKRDED CCCCCEECCCCCCCC	5.73	28526873
214	S-nitrosylation	PNVLPVQCTGKRDED CCCCCEECCCCCCCC	5.73	24895380
215	Phosphorylation	NVLPVQCTGKRDEDK CCCCEECCCCCCCCC	28.75	25195567
217	Ubiquitination	LPVQCTGKRDEDKDK CCEECCCCCCCCCCC	38.22	22790023
217	Acetylation	LPVQCTGKRDEDKDK CCEECCCCCCCCCCC	38.22	14496147
254	Ubiquitination	YGKLLQPKYLQPLLA CCCCCCCHHHHHEEE	45.70	-
266	N-linked_Glycosylation	LLAVQFTNLTVDTEI EEEEEEECCEECCEE	34.70	19349973
289	Ubiquitination	ENIGYSEKDRFQGRF CCCCCCHHHCCCCEE	48.54	-
289	Acetylation	ENIGYSEKDRFQGRF CCCCCCHHHCCCCEE	48.54	23954790
289	Succinylation	ENIGYSEKDRFQGRF CCCCCCHHHCCCCEE	48.54	23954790

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
Oops, there are no upstream regulatory protein records of AT1B1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AT1B1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of AT1B1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of AT1B1_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-158; ASN-163 AND ASN-266,AND MASS SPECTROMETRY.	19349973 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-101, AND MASSSPECTROMETRY.	18034455 [Abstract]