dbPTM

MIER3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MIER3_HUMAN
UniProt AC	Q7Z3K6
Protein Name	Mesoderm induction early response protein 3
Gene Name	MIER3
Organism	Homo sapiens (Human).
Sequence Length	550
Subcellular Localization	Nucleus .
Protein Description	Transcriptional repressor..
Protein Sequence	MAEASFGSSSPVGSLSSEDHDFDPTAEMLVHDYDDERTLEEEEMMDEGKNFSSEIEDLEKEGTMPLEDLLAFYGYEPTIPAVANSSANSSPSELADELPDMTLDKEEIAKDLLSGDDEETQSSADDLTPSVTSHETSDFFPRPLRSNTACDGDKESEVEDVETDSGNSPEDLRKEIMIGLQYQAEIPPYLGEYDGNEKVYENEDQLLWCPDVVLESKVKEYLVETSLRTGSEKIMDRISAGTHTRDNEQALYELLKCNHNIKEAIERYCCNGKASQEGMTAWTEEECRSFEHALMLFGKDFHLIQKNKVRTRTVAECVAFYYMWKKSERYDYFAQQTRFGKKRYNHHPGVTDYMDRLVDETEALGGTVNASALTSNRPEPIPDQQLNILNSFTASDLTALTNSVATVCDPTDVNCLDDSFPPLGNTPRGQVNHVPVVTEELLTLPSNGESDCFNLFETGFYHSELNPMNMCSEESERPAKRLKMGIAVPESFMNEVSVNNLGVDFENHTHHITSAKMAVSVADFGSLSANETNGFISAHALHQHAALHSE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MAEASFGSSSPV ---CCCCCCCCCCCC	22.96	28122231
8	Phosphorylation	MAEASFGSSSPVGSL CCCCCCCCCCCCCCC	26.15	28348404
9	Phosphorylation	AEASFGSSSPVGSLS CCCCCCCCCCCCCCC	38.75	28348404
10	Phosphorylation	EASFGSSSPVGSLSS CCCCCCCCCCCCCCC	25.87	25921289
14	Phosphorylation	GSSSPVGSLSSEDHD CCCCCCCCCCCCCCC	25.88	28348404
16	Phosphorylation	SSPVGSLSSEDHDFD CCCCCCCCCCCCCCC	33.12	28348404
17	Phosphorylation	SPVGSLSSEDHDFDP CCCCCCCCCCCCCCC	52.95	28348404
33	Phosphorylation	AEMLVHDYDDERTLE HHHEEECCCCCCCCC	15.49	18083107
38	Phosphorylation	HDYDDERTLEEEEMM ECCCCCCCCCHHHHH	36.15	27499020
52	Phosphorylation	MDEGKNFSSEIEDLE HHCCCCCHHHHHHHH	36.13	26503892
53	Phosphorylation	DEGKNFSSEIEDLEK HCCCCCHHHHHHHHH	38.16	26503892
114	Phosphorylation	EIAKDLLSGDDEETQ HHHHHHHCCCCHHHH	47.69	21082442
120	Phosphorylation	LSGDDEETQSSADDL HCCCCHHHHCCHHHC	31.53	23663014
122	Phosphorylation	GDDEETQSSADDLTP CCCHHHHCCHHHCCC	34.61	23663014
123	Phosphorylation	DDEETQSSADDLTPS CCHHHHCCHHHCCCC	26.37	23663014
128	Phosphorylation	QSSADDLTPSVTSHE HCCHHHCCCCCCCCC	22.10	23663014
130	Phosphorylation	SADDLTPSVTSHETS CHHHCCCCCCCCCCC	32.56	23663014
132	Phosphorylation	DDLTPSVTSHETSDF HHCCCCCCCCCCCCC	28.80	23663014
133	Phosphorylation	DLTPSVTSHETSDFF HCCCCCCCCCCCCCC	19.71	23663014
136	Phosphorylation	PSVTSHETSDFFPRP CCCCCCCCCCCCCCC	28.33	20873877
137	Phosphorylation	SVTSHETSDFFPRPL CCCCCCCCCCCCCCC	29.45	20873877
146	Phosphorylation	FFPRPLRSNTACDGD CCCCCCCCCCCCCCC	46.33	28450419
148	Phosphorylation	PRPLRSNTACDGDKE CCCCCCCCCCCCCCC	29.88	30278072
156	Phosphorylation	ACDGDKESEVEDVET CCCCCCCHHCEECCC	53.32	23401153
163	Phosphorylation	SEVEDVETDSGNSPE HHCEECCCCCCCCHH	35.00	25159151
165	Phosphorylation	VEDVETDSGNSPEDL CEECCCCCCCCHHHH	47.49	30576142
168	Phosphorylation	VETDSGNSPEDLRKE CCCCCCCCHHHHHHH	32.94	25849741
217	Ubiquitination	PDVVLESKVKEYLVE CHHHHHHHHHHHHHH	48.20	29967540
222	Ubiquitination	ESKVKEYLVETSLRT HHHHHHHHHHHHCCC	2.69	29967540
233	Acetylation	SLRTGSEKIMDRISA HCCCCCHHHHHHHHC	45.06	25953088
252	Phosphorylation	RDNEQALYELLKCNH CCHHHHHHHHHHCCC	13.93	-
256	Ubiquitination	QALYELLKCNHNIKE HHHHHHHHCCCCHHH	45.69	29967540
257 (in isoform 2)	Phosphorylation	-	6.72	25147952
261	Ubiquitination	LLKCNHNIKEAIERY HHHCCCCHHHHHHHH	3.12	29967540
262	Ubiquitination	LKCNHNIKEAIERYC HHCCCCHHHHHHHHC	46.54	29967540
267	Ubiquitination	NIKEAIERYCCNGKA CHHHHHHHHCCCCCC	24.55	29967540
299	Acetylation	HALMLFGKDFHLIQK HHHHHHCCCEEHHCC	50.30	19820991
305	Ubiquitination	GKDFHLIQKNKVRTR CCCEEHHCCCCCCHH	50.02	29967540
306	Ubiquitination	KDFHLIQKNKVRTRT CCEEHHCCCCCCHHH	52.31	29967540
311	Ubiquitination	IQKNKVRTRTVAECV HCCCCCCHHHHHHHH	33.41	29967540
332	Phosphorylation	KKSERYDYFAQQTRF HHHHHHCHHHHHCHH	7.59	-

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 MIER3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MIER3_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 MIER3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MIER3_HUMAN !!

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 MIER3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-53, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-156, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASSSPECTROMETRY.	16565220 [Abstract]