AMERL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AMERL_HUMAN
• UniProt AC: Q6DCA0
• Protein Name: AMMECR1-like protein
• Gene Name: AMMECR1L
• Organism: Homo sapiens (Human).
• Sequence Length: 310
• Protein Sequence: MGKRRCVPPLEPKLAAGCCGVKKPKLSGSGTHSHGNQSTTVPGSSSGPLQNHQHVDSSSGRENVSDLTLGPGNSPITRMNPASGALSPLPRPNGTANTTKNLVVTAEMCCYCFDVLYCHLYGFPQPRLPRFTNDPYPLFVTWKTGRDKRLRGCIGTFSAMNLHSGLREYTLTSALKDSRFPPLTREELPKLFCSVSLLTNFEDASDYLDWEVGVHGIRIEFINEKGVKRTATYLPEVAKEQDWDQIQTIDSLLRKGGFKAPITSEFRKTIKLTRYRSEKVTISYAEYIASRQHCFQNGTLHAPPLYNHYS

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
22	Acetylation	AAGCCGVKKPKLSGS CCCCCCCCCCCCCCC	48.95	25953088
22	Sumoylation	AAGCCGVKKPKLSGS CCCCCCCCCCCCCCC	48.95	-
22	Sumoylation	AAGCCGVKKPKLSGS CCCCCCCCCCCCCCC	48.95	-
27	Phosphorylation	GVKKPKLSGSGTHSH CCCCCCCCCCCCCCC	36.72	29449344
29	Phosphorylation	KKPKLSGSGTHSHGN CCCCCCCCCCCCCCC	36.82	29449344
31	Phosphorylation	PKLSGSGTHSHGNQS CCCCCCCCCCCCCCC	23.15	29449344
33	Phosphorylation	LSGSGTHSHGNQSTT CCCCCCCCCCCCCCC	32.69	29449344
38	Phosphorylation	THSHGNQSTTVPGSS CCCCCCCCCCCCCCC	30.00	28555341
39	Phosphorylation	HSHGNQSTTVPGSSS CCCCCCCCCCCCCCC	23.27	29449344
40	Phosphorylation	SHGNQSTTVPGSSSG CCCCCCCCCCCCCCC	29.92	29449344
65	Phosphorylation	SSGRENVSDLTLGPG CCCCCCHHHCCCCCC	38.18	29255136
68	Phosphorylation	RENVSDLTLGPGNSP CCCHHHCCCCCCCCC	34.36	29255136
74	Phosphorylation	LTLGPGNSPITRMNP CCCCCCCCCCCCCCC	24.48	23401153
77	Phosphorylation	GPGNSPITRMNPASG CCCCCCCCCCCCCCC	27.53	29255136
83	Phosphorylation	ITRMNPASGALSPLP CCCCCCCCCCCCCCC	26.34	22199227
87	Phosphorylation	NPASGALSPLPRPNG CCCCCCCCCCCCCCC	24.69	22199227
95	Phosphorylation	PLPRPNGTANTTKNL CCCCCCCCCCCCCCE	24.31	22199227
98	Phosphorylation	RPNGTANTTKNLVVT CCCCCCCCCCCEEEE	36.36	22199227
99	Phosphorylation	PNGTANTTKNLVVTA CCCCCCCCCCEEEEH	20.10	22199227
143	Ubiquitination	YPLFVTWKTGRDKRL CCEEEEEECCCCCCC	31.56	-
169	Phosphorylation	LHSGLREYTLTSALK CCCCCCEEEHHHHHC	10.70	26074081
176	Ubiquitination	YTLTSALKDSRFPPL EEHHHHHCCCCCCCC	54.07	-
184	Phosphorylation	DSRFPPLTREELPKL CCCCCCCCHHHHHHH	41.63	68705173
225	Ubiquitination	RIEFINEKGVKRTAT EEEEECCCCCCEEEE	65.60	-
239	Ubiquitination	TYLPEVAKEQDWDQI ECCHHHHHHCCHHHH	62.17	-
251	Phosphorylation	DQIQTIDSLLRKGGF HHHHHHHHHHHCCCC	26.00	24719451
255	Ubiquitination	TIDSLLRKGGFKAPI HHHHHHHCCCCCCCC	64.45	-
264	Phosphorylation	GFKAPITSEFRKTIK CCCCCCCHHHHHHEE	35.14	72550369
269	Phosphorylation	ITSEFRKTIKLTRYR CCHHHHHHEEEEECC	21.06	46162943

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AMERL_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 AMERL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MACF1_HUMAN	MACF1	physical	26186194
FNTA_HUMAN	FNTA	physical	26186194
PGTB1_HUMAN	PGGT1B	physical	26186194
PGTB1_HUMAN	PGGT1B	physical	28514442
FNTA_HUMAN	FNTA	physical	28514442
MACF1_HUMAN	MACF1	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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.
PubMed: 19690332

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.
PubMed: 18669648