dbPTM

ACE2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACE2_HUMAN
UniProt AC	Q9BYF1
Protein Name	Angiotensin-converting enzyme 2
Gene Name	ACE2
Organism	Homo sapiens (Human).
Sequence Length	805
Subcellular Localization	Processed angiotensin-converting enzyme 2: Secreted. Cell membrane Single-pass type I membrane protein. Cytoplasm. Detected in both cell membrane and cytoplasm in neurons..
Protein Description	Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function.; (Microbial infection) Acts as a receptor for SARS coronavirus/SARS-CoV.; (Microbial infection) Acts as a receptor for Human coronavirus NL63/HCoV-NL63..
Protein Sequence	MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSSSWLLL ------CCCHHHHHH	38.64	46157543
10	Phosphorylation	SSSWLLLSLVAVTAA CHHHHHHHHHHHHHH	22.29	46157537
20	Phosphorylation	AVTAAQSTIEEQAKT HHHHHHHHHHHHHHH	21.96	29116813
27	Phosphorylation	TIEEQAKTFLDKFNH HHHHHHHHHHHHCCH	32.23	29116813
53	N-linked_Glycosylation	ASWNYNTNITEENVQ HHCCCCCCCCHHHHH	35.23	14754895
90	N-linked_Glycosylation	YPLQEIQNLTVKLQL CCHHHHHHHHHHHHH	43.25	15084671
103	N-linked_Glycosylation	QLQALQQNGSSVLSE HHHHHHHCCCCCCCC	39.08	14754895
128	Phosphorylation	NTMSTIYSTGKVCNP HHHHHHHHCCCCCCC	27.17	68717163
129	Phosphorylation	TMSTIYSTGKVCNPD HHHHHHHCCCCCCCC	24.85	68717169
322	N-linked_Glycosylation	FVSVGLPNMTQGFWE HHHCCCCCCCCCCHH	51.69	14754895
432	N-linked_Glycosylation	SPDFQEDNETEINFL CCCCCCCCHHHHHHH	58.29	14754895
449	Phosphorylation	QALTIVGTLPFTYML HHHHHHHCCCHHHHH	21.99	22210691
453	Phosphorylation	IVGTLPFTYMLEKWR HHHCCCHHHHHHHEE	13.19	22210691
545	Phosphorylation	PLHKCDISNSTEAGQ CCCCCCCCCCCHHHH	16.10	51457809
546	N-linked_Glycosylation	LHKCDISNSTEAGQK CCCCCCCCCCHHHHH	53.97	14754895
547	Phosphorylation	HKCDISNSTEAGQKL CCCCCCCCCHHHHHH	22.34	51457815
548	Phosphorylation	KCDISNSTEAGQKLF CCCCCCCCHHHHHHH	33.82	51457821
625	Ubiquitination	IKVRISLKSALGDKA EEEEEEHHHHHCCCE	27.22	33845483
676	Ubiquitination	DVRVANLKPRISFNF CEEECCCCCCEEEEE	31.86	29967540
690	N-linked_Glycosylation	FFVTAPKNVSDIIPR EEEECCCCHHHCCCH	37.15	UniProtKB CARBOHYD
692	Phosphorylation	VTAPKNVSDIIPRTE EECCCCHHHCCCHHH	32.27	46157549
702	Ubiquitination	IPRTEVEKAIRMSRS CCHHHHHHHHHHHHH	55.05	33845483
770	Acetylation	TGIRDRKKKNKARSG HCCCCHHHHCCCCCC	63.57	2520697
771	Acetylation	GIRDRKKKNKARSGE CCCCHHHHCCCCCCC	67.71	2520705
773	Acetylation	RDRKKKNKARSGENP CCHHHHCCCCCCCCC	54.80	2520713
776	Phosphorylation	KKKNKARSGENPYAS HHHCCCCCCCCCCCE	56.15	28857561
781	Phosphorylation	ARSGENPYASIDISK CCCCCCCCCEEECCC	25.27	26657352
783	Phosphorylation	SGENPYASIDISKGE CCCCCCCEEECCCCC	18.23	26657352
787	Phosphorylation	PYASIDISKGENNPG CCCEEECCCCCCCCC	30.75	28442448

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
787	S	Phosphorylation	Kinase	CK2A1	P68400	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
90	N	Glycosylation		15084671
N-glycosylation on Asn-90 may limit SARS infectivity.

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 ACE2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANGT_HUMAN	AGT	physical	10969042
ANGT_HUMAN	AGT	physical	15283675
ACE2_HUMAN	ACE2	physical	16166518
CATA_HUMAN	CAT	physical	26344197
INO1_HUMAN	ISYNA1	physical	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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ACE2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"ACE2 X-ray structures reveal a large hinge-bending motion importantfor inhibitor binding and catalysis."; Towler P., Staker B., Prasad S.G., Menon S., Tang J., Parsons T.,Ryan D., Fisher M., Williams D., Dales N.A., Patane M.A.,Pantoliano M.W.; J. Biol. Chem. 279:17996-18007(2004). Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-615, X-RAY CRYSTALLOGRAPHY(3.0 ANGSTROMS) OF 19-615 IN COMPLEX WITH MLN-4760, DISULFIDE BONDS,AND GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 ANDASN-546.	14754895 [Abstract]
"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-546, AND MASSSPECTROMETRY.	19159218 [Abstract]
"A proteomic analysis of human bile."; Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; Mol. Cell. Proteomics 3:715-728(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90, AND MASS SPECTROMETRY.	15084671 [Abstract]

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