dbPTM

EPMIP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EPMIP_HUMAN
UniProt AC	Q7L775
Protein Name	EPM2A-interacting protein 1
Gene Name	EPM2AIP1
Organism	Homo sapiens (Human).
Sequence Length	607
Subcellular Localization	Endoplasmic reticulum .
Protein Description
Protein Sequence	MWMTPKRSKMEVDEALVFRPEWTQRYLVVEPPEGDGALCLVCRRLIVATRERDVRRHYEAEHEYYERYVADGERAALVERLRQGDLPVASFTPEERAARAGLGLCRLLALKGRGWGEGDFVYQCMEVLLREVLPEHVSVLQGVDLSPDITRQRILSIDRNLRNQLFNRARDFKAYSLALDDQAFVAYENYLLVFIRGVGPELEVQEDLLTIINLTHHFSVGALMSAILESLQTAGLSLQRMVGLTTTHTLRMIGENSGLVSYMREKAVSPNCWNVIHYSGFLHLELLSSYDVDVNQIINTISEWIVLIKTRGVRRPEFQTLLTESESEHGERVNGRCLNNWLRRGKTLKLIFSLRKEMEAFLVSVGATTVHFSDKQWLCDFGFLVDIMEHLRELSEELRVSKVFAAAAFDHICTFEVKLNLFQRHIEEKNLTDFPALREVVDELKQQNKEDEKIFDPDRYQMVICRLQKEFERHFKDLRFIKKDLELFSNPFNFKPEYAPISVRVELTKLQANTNLWNEYRIKDLGQFYAGLSAESYPIIKGVACKVASLFDSNQICEKAFSYLTRNQHTLSQPLTDEHLQALFRVATTEMEPGWDDLVRERNESNP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MWMTPKRSKME ----CCCCCCCCCCC	15.33	24719451
49	Phosphorylation	CRRLIVATRERDVRR CHHHHHHCCHHHHHH	23.36	-
64	Phosphorylation	HYEAEHEYYERYVAD HHHHHHHHHHHHCCC	16.72	-
90	Phosphorylation	QGDLPVASFTPEERA CCCCCCCCCCHHHHH	29.86	28555341
92	Phosphorylation	DLPVASFTPEERAAR CCCCCCCCHHHHHHH	27.56	21815630
111	Acetylation	LCRLLALKGRGWGEG HHHHHHHCCCCCCCC	40.74	25953088
111	Ubiquitination	LCRLLALKGRGWGEG HHHHHHHCCCCCCCC	40.74	-
146	Phosphorylation	VLQGVDLSPDITRQR HHCCCCCCCCCCHHH	18.96	30278072
150	Phosphorylation	VDLSPDITRQRILSI CCCCCCCCHHHHHHH	28.29	28122231
156	Phosphorylation	ITRQRILSIDRNLRN CCHHHHHHHCHHHHH	21.77	24719451
237	Phosphorylation	SLQTAGLSLQRMVGL HHHHCCCCHHHHHCC	22.87	24719451
356	Ubiquitination	KLIFSLRKEMEAFLV HHHHHHHHHHHHHHH	67.70	30230243
373	Phosphorylation	GATTVHFSDKQWLCD CCEEEECCCCCEEHH	29.08	22468782
429	Ubiquitination	FQRHIEEKNLTDFPA HHHHHHHCCCCCCHH	44.46	29967540
445	Ubiquitination	REVVDELKQQNKEDE HHHHHHHHHCCCHHC	48.03	29967540
453	Ubiquitination	QQNKEDEKIFDPDRY HCCCHHCCCCCHHHH	62.08	29967540
460	Phosphorylation	KIFDPDRYQMVICRL CCCCHHHHHHHHHHH	14.35	18083107
469	Ubiquitination	MVICRLQKEFERHFK HHHHHHHHHHHHHHC	69.80	32142685
469	Acetylation	MVICRLQKEFERHFK HHHHHHHHHHHHHHC	69.80	23749302
495	Ubiquitination	FSNPFNFKPEYAPIS HCCCCCCCCCCCCCE	37.74	21890473
523	Ubiquitination	LWNEYRIKDLGQFYA CCCEEEECCHHHHHC	37.59	21890473
546	Ubiquitination	IIKGVACKVASLFDS CHHHHHHHHHHHCCH	30.97	29967540
559	Ubiquitination	DSNQICEKAFSYLTR CHHHHHHHHHHHHHC	50.77	21987572
605	Phosphorylation	LVRERNESNP----- HHHHHHCCCC-----	58.93	19845377

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 EPMIP_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPMIP_HUMAN	EPM2AIP1	physical	25416956
PRDC1_HUMAN	PRTFDC1	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
CIP1_HUMAN	CCNB1IP1	physical	25416956
CA050_HUMAN	C1orf50	physical	25416956
CPSF7_HUMAN	CPSF7	physical	25416956
KCTD1_HUMAN	KCTD1	physical	25416956
ZSC18_HUMAN	ZSCAN18	physical	28514442
DHX40_HUMAN	DHX40	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.

Regulatory Network of EPMIP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASSSPECTROMETRY.	18691976 [Abstract]