dbPTM

ERP29_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ERP29_HUMAN
UniProt AC	P30040
Protein Name	Endoplasmic reticulum resident protein 29
Gene Name	ERP29
Organism	Homo sapiens (Human).
Sequence Length	261
Subcellular Localization	Endoplasmic reticulum lumen. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description	Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER..
Protein Sequence	MAAAVPRAAFLSPLLPLLLGFLLLSAPHGGSGLHTKGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSASSDDLLVAEVGISDYGDKLNMELSEKYKLDKESYPVFYLFRDGDFENPVPYTGAVKVGAIQRWLKGQGVYLGMPGCLPVYDALAGEFIRASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGKKEELQKSLNILTAFQKKGAEKEEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	Phosphorylation	PLDTVTFYKVIPKSK CCCEEEEEEEEECCC	8.59	-
48	Ubiquitination	LDTVTFYKVIPKSKF CCEEEEEEEEECCCE	29.51	21890473
48	2-Hydroxyisobutyrylation	LDTVTFYKVIPKSKF CCEEEEEEEEECCCE	29.51	-
54	Acetylation	YKVIPKSKFVLVKFD EEEEECCCEEEEEEE	45.69	27452117
54	2-Hydroxyisobutyrylation	YKVIPKSKFVLVKFD EEEEECCCEEEEEEE	45.69	-
62	Phosphorylation	FVLVKFDTQYPYGEK EEEEEEECCCCCCCC	32.89	28152594
64	Phosphorylation	LVKFDTQYPYGEKQD EEEEECCCCCCCCHH	10.66	25367160
66	Phosphorylation	KFDTQYPYGEKQDEF EEECCCCCCCCHHHH	32.74	21082442
69	Ubiquitination	TQYPYGEKQDEFKRL CCCCCCCCHHHHHHH	59.70	-
69	2-Hydroxyisobutyrylation	TQYPYGEKQDEFKRL CCCCCCCCHHHHHHH	59.70	-
80	Phosphorylation	FKRLAENSASSDDLL HHHHHHCCCCCCCEE	22.49	-
83	Phosphorylation	LAENSASSDDLLVAE HHHCCCCCCCEEEEE	34.56	-
102	Sulfoxidation	DYGDKLNMELSEKYK CHHHHHCHHHHHHHC	8.75	28465586
105	Phosphorylation	DKLNMELSEKYKLDK HHHCHHHHHHHCCCH	20.80	26074081
107	2-Hydroxyisobutyrylation	LNMELSEKYKLDKES HCHHHHHHHCCCHHH	44.29	-
107	Acetylation	LNMELSEKYKLDKES HCHHHHHHHCCCHHH	44.29	26822725
108	Phosphorylation	NMELSEKYKLDKESY CHHHHHHHCCCHHHC	16.84	26074081
112	2-Hydroxyisobutyrylation	SEKYKLDKESYPVFY HHHHCCCHHHCCEEE	60.02	-
114	Phosphorylation	KYKLDKESYPVFYLF HHCCCHHHCCEEEEE	40.24	20068231
115	Phosphorylation	YKLDKESYPVFYLFR HCCCHHHCCEEEEEE	12.42	20068231
119	Phosphorylation	KESYPVFYLFRDGDF HHHCCEEEEEECCCC	12.74	-
122	Methylation	YPVFYLFRDGDFENP CCEEEEEECCCCCCC	44.39	-
132	Phosphorylation	DFENPVPYTGAVKVG CCCCCCCCCCCCHHH	20.31	28152594
133	Phosphorylation	FENPVPYTGAVKVGA CCCCCCCCCCCHHHH	16.76	28152594
137	Ubiquitination	VPYTGAVKVGAIQRW CCCCCCCHHHHHHHH	34.12	-
137	2-Hydroxyisobutyrylation	VPYTGAVKVGAIQRW CCCCCCCHHHHHHHH	34.12	-
182	2-Hydroxyisobutyrylation	EARQALLKQGQDNLS HHHHHHHHHCCCCHH	53.91	-
182	Ubiquitination	EARQALLKQGQDNLS HHHHHHHHHCCCCHH	53.91	21890473
189	Phosphorylation	KQGQDNLSSVKETQK HHCCCCHHHHHHHHH	39.06	28102081
190	Phosphorylation	QGQDNLSSVKETQKK HCCCCHHHHHHHHHH	40.13	28102081
192	Ubiquitination	QDNLSSVKETQKKWA CCCHHHHHHHHHHHH	57.92	-
192	Succinylation	QDNLSSVKETQKKWA CCCHHHHHHHHHHHH	57.92	23954790
192	Acetylation	QDNLSSVKETQKKWA CCCHHHHHHHHHHHH	57.92	27452117
204	2-Hydroxyisobutyrylation	KWAEQYLKIMGKILD HHHHHHHHHHHHHHH	26.22	-
204	Acetylation	KWAEQYLKIMGKILD HHHHHHHHHHHHHHH	26.22	27452117
219	Phosphorylation	QGEDFPASEMTRIAR CCCCCCHHHHHHHHH	28.30	20068231
221	Sulfoxidation	EDFPASEMTRIARLI CCCCHHHHHHHHHHH	2.57	21406390
222	Phosphorylation	DFPASEMTRIARLIE CCCHHHHHHHHHHHH	18.18	20068231
234	Phosphorylation	LIEKNKMSDGKKEEL HHHHCCCCCCCHHHH	44.83	30001349
243	Ubiquitination	GKKEELQKSLNILTA CCHHHHHHHHHHHHH	70.32	21890473
243	Acetylation	GKKEELQKSLNILTA CCHHHHHHHHHHHHH	70.32	23236377
244	Phosphorylation	KKEELQKSLNILTAF CHHHHHHHHHHHHHH	17.43	21712546
249	Phosphorylation	QKSLNILTAFQKKGA HHHHHHHHHHHHCCC	22.94	25022875
253	2-Hydroxyisobutyrylation	NILTAFQKKGAEKEE HHHHHHHHCCCCCCC	46.88	-

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
64	Y	Phosphorylation	Kinase	PKDCC	Q504Y2	Uniprot
66	Y	Phosphorylation	Kinase	PKDCC	Q504Y2	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ERP29_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 ERP29_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSPB1_HUMAN	HSPB1	physical	26344197
UBCP1_HUMAN	UBLCP1	physical	26344197
GLB1L_HUMAN	GLB1L	physical	28514442
A16A1_HUMAN	ALDH16A1	physical	28514442
ARSB_HUMAN	ARSB	physical	28514442
DEOC_HUMAN	DERA	physical	28514442
EXOC5_HUMAN	EXOC5	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 ERP29_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64 AND TYR-66, AND MASSSPECTROMETRY.	18083107 [Abstract]