ASNA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ASNA_HUMAN
• UniProt AC: O43681
• Protein Name: ATPase ASNA1 {ECO:0000255|HAMAP-Rule:MF_03112}
• Gene Name: ASNA1 {ECO:0000255|HAMAP-Rule:MF_03112}
• Organism: Homo sapiens (Human).
• Sequence Length: 348
• Subcellular Localization: Cytoplasm. Endoplasmic reticulum. Nucleus, nucleolus.
• Protein Description: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting (By similarity). May be involved in insulin signaling..
• Protein Sequence: MAAGVAGWGVEAEEFEDAPDVEPLEPTLSNIIEQRSLKWIFVGGKGGVGKTTCSCSLAVQLSKGRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCKIDTHNIIVNQLVFPDPEKPCKMCEARHKIQAKYLDQMEDLYEDFHIVKLPLLPHEVRGADKVNTFSALLLEPYKPPSAQ

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
45	Acetylation	KWIFVGGKGGVGKTT EEEEECCCCCCCCCC	46.71	26051181
63	Acetylation	SLAVQLSKGRESVLI EEEEECCCCCCEEEE	71.26	26051181
267	Acetylation	RLIQELAKCKIDTHN HHHHHHHCCCCCCCC	49.00	26051181

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ASNA_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ASNA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S61A1_HUMAN	SEC61A1	physical	20676083
VAMP2_HUMAN	VAMP2	physical	20676083
STX5_HUMAN	STX5	physical	20676083
TBB5_HUMAN	TUBB	physical	22863883
VAPB_HUMAN	VAPB	physical	24885147
UBC_HUMAN	UBC	physical	24885147
BAG6_HUMAN	BAG6	physical	24885147
FAF1_HUMAN	FAF1	physical	24885147
APEL_HUMAN	APLN	physical	22505607
STAT_HUMAN	STATH	physical	22505607
SC61B_HUMAN	SEC61B	physical	22505607
ASPH_HUMAN	ASPH	physical	25416956
GPX7_HUMAN	GPX7	physical	25416956
HLPDA_HUMAN	HILPDA	physical	25416956
PSA2_HUMAN	PSMA2	physical	26344197
PSA4_HUMAN	PSMA4	physical	26344197
GET4_HUMAN	GET4	physical	21516116
WRB_HUMAN	WRB	physical	28514442
ZN579_HUMAN	ZNF579	physical	28514442
ASPC1_HUMAN	ASPSCR1	physical	28514442
NUDT9_HUMAN	NUDT9	physical	28514442

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
• There are no disease associations of PTM sites.
• DrugBank
• DB00171: Adenosine triphosphate

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330