dbPTM

GRL1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRL1A_HUMAN
UniProt AC	P0CAP2
Protein Name	DNA-directed RNA polymerase II subunit GRINL1A
Gene Name	POLR2M
Organism	Homo sapiens (Human).
Sequence Length	368
Subcellular Localization	Isoform 1: Nucleus .
Protein Description	Isoform 1 appears to be a stable component of the Pol II(G) complex form of RNA polymerase II (Pol II). Pol II synthesizes mRNA precursors and many functional non-coding RNAs and is the central component of the basal RNA polymerase II transcription machinery. Isoform 1 may play a role in the Mediator complex-dependent regulation of transcription activation. Isoform 1 acts in vitro as a negative regulator of transcriptional activation; this repression is relieved by the Mediator complex, which restores Pol II(G) activator-dependent transcription to a level equivalent to that of Pol II..
Protein Sequence	MCSLPRGFEPQAPEDLAQRSLVELREMLKRQERLLRNEKFICKLPDKGKKIFDSFAKLKAAIAECEEVRRKSELFNPVSLDCKLRQKAIAEVDVGTDKAQNSDPILDTSSLVPGCSSVDNIKSSQTSQNQGLGRPTLEGDEETSEVEYTVNKGPASSNRDRVPPSSEASEHHPRHRVSSQAEDTSSSFDNLFIDRLQRITIADQGEQQSEENASTKNLTGLSSGTEKKPHYMEVLEMRAKNPVPQLRKFKTNVLPFRQNDSSSHCQKSGSPISSEERRRRDKQHLDDITAARLLPLHHMPTQLLSIEESLALQKQQKQNYEEMQAKLAAQKLAERLNIKMRSYNPEGESSGRYREVRDEDDDWSSDEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
71	Ubiquitination	ECEEVRRKSELFNPV HHHHHHHHHHHCCCC	37.40	-
72	Phosphorylation	CEEVRRKSELFNPVS HHHHHHHHHHCCCCC	37.41	23401153
79	Phosphorylation	SELFNPVSLDCKLRQ HHHCCCCCCCHHHCH	21.53	23312004
83	Ubiquitination	NPVSLDCKLRQKAIA CCCCCCHHHCHHHEE	46.50	-
109	Phosphorylation	SDPILDTSSLVPGCS CCCCCCHHHCCCCCC	22.72	25627689
110	Phosphorylation	DPILDTSSLVPGCSS CCCCCHHHCCCCCCC	35.16	25627689
123	Phosphorylation	SSVDNIKSSQTSQNQ CCHHHHHCCCCCCCC	24.71	26270265
124	Phosphorylation	SVDNIKSSQTSQNQG CHHHHHCCCCCCCCC	32.26	26270265
126	Phosphorylation	DNIKSSQTSQNQGLG HHHHCCCCCCCCCCC	33.94	26270265
127	Phosphorylation	NIKSSQTSQNQGLGR HHHCCCCCCCCCCCC	21.35	26270265
136	Phosphorylation	NQGLGRPTLEGDEET CCCCCCCCCCCCCCC	35.76	28796482
143	Phosphorylation	TLEGDEETSEVEYTV CCCCCCCCEEEEEEE	28.30	28796482
144	Phosphorylation	LEGDEETSEVEYTVN CCCCCCCEEEEEEEE	42.81	28796482
148	Phosphorylation	EETSEVEYTVNKGPA CCCEEEEEEEECCCC	22.59	28796482
149	Phosphorylation	ETSEVEYTVNKGPAS CCEEEEEEEECCCCC	12.23	28796482
157	Phosphorylation	VNKGPASSNRDRVPP EECCCCCCCCCCCCC	37.68	-
165	Phosphorylation	NRDRVPPSSEASEHH CCCCCCCCCHHHHCC	34.44	27732954
166	Phosphorylation	RDRVPPSSEASEHHP CCCCCCCCHHHHCCC	42.85	27732954
166	O-linked_Glycosylation	RDRVPPSSEASEHHP CCCCCCCCHHHHCCC	42.85	30379171
169	Phosphorylation	VPPSSEASEHHPRHR CCCCCHHHHCCCCCC	33.15	27732954
178	Phosphorylation	HHPRHRVSSQAEDTS CCCCCCCCCCCCCCC	19.38	23401153
179	Phosphorylation	HPRHRVSSQAEDTSS CCCCCCCCCCCCCCC	30.47	23401153
184	Phosphorylation	VSSQAEDTSSSFDNL CCCCCCCCCCCCHHH	23.24	27794612
185	Phosphorylation	SSQAEDTSSSFDNLF CCCCCCCCCCCHHHH	35.99	21082442
186	Phosphorylation	SQAEDTSSSFDNLFI CCCCCCCCCCHHHHH	36.80	30108239
187	Phosphorylation	QAEDTSSSFDNLFID CCCCCCCCCHHHHHH	36.06	30108239
209	Phosphorylation	ADQGEQQSEENASTK CCCCCHHCHHHHCCC	46.72	-
214	Phosphorylation	QQSEENASTKNLTGL HHCHHHHCCCCCCCC	52.04	-
215	Phosphorylation	QSEENASTKNLTGLS HCHHHHCCCCCCCCC	22.88	-
216	Ubiquitination	SEENASTKNLTGLSS CHHHHCCCCCCCCCC	47.68	-
222	Phosphorylation	TKNLTGLSSGTEKKP CCCCCCCCCCCCCCC	28.24	-
268	Phosphorylation	SSSHCQKSGSPISSE CCCCCHHCCCCCCHH	20.72	29255136
270	Phosphorylation	SHCQKSGSPISSEER CCCHHCCCCCCHHHH	26.59	23401153
273	Phosphorylation	QKSGSPISSEERRRR HHCCCCCCHHHHHHH	34.77	23403867
274	Phosphorylation	KSGSPISSEERRRRD HCCCCCCHHHHHHHH	44.17	23403867
282	Ubiquitination	EERRRRDKQHLDDIT HHHHHHHHHCHHHHH	37.49	-
326	Ubiquitination	NYEEMQAKLAAQKLA CHHHHHHHHHHHHHH	23.05	-
332 (in isoform 3)	Phosphorylation	-	3.88	20068231
333 (in isoform 3)	Phosphorylation	-	13.60	20068231
338 (in isoform 3)	Phosphorylation	-	4.37	20068231
346 (in isoform 3)	Phosphorylation	-	72.46	20068231
353	Phosphorylation	EGESSGRYREVRDED CCCCCCCCEECCCCC	18.04	21406692
356 (in isoform 3)	Phosphorylation	-	7.46	20068231
364	Phosphorylation	RDEDDDWSSDEF--- CCCCCCCCCCCC---	34.60	22617229
365	Phosphorylation	DEDDDWSSDEF---- CCCCCCCCCCC----	36.58	22617229

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 GRL1A_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GRL1A_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 GRL1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HIG1B_HUMAN	HIGD1B	physical	16169070
AHSP_HUMAN	AHSP	physical	16169070
WDR89_HUMAN	WDR89	physical	16169070
ANKH1_HUMAN	ANKHD1	physical	16169070
MYO3A_HUMAN	MYO3A	physical	16169070
MYO9A_HUMAN	MYO9A	physical	16169070
QCR8_HUMAN	UQCRQ	physical	16169070
SCMH1_HUMAN	SCMH1	physical	16169070
ZN410_HUMAN	ZNF410	physical	16169070
APOD_HUMAN	APOD	physical	16169070
DGKZ_HUMAN	DGKZ	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
RBM4B_HUMAN	RBM4B	physical	16169070
PRS7_HUMAN	PSMC2	physical	16169070
RL7A_HUMAN	RPL7A	physical	16169070
RPB7_HUMAN	POLR2G	physical	26186194
RPAP1_HUMAN	RPAP1	physical	26186194
RPAP2_HUMAN	RPAP2	physical	26186194
UBP47_HUMAN	USP47	physical	26186194
RPB1_HUMAN	POLR2A	physical	26186194
RPB4_HUMAN	POLR2D	physical	26186194
RPR1A_HUMAN	RPRD1A	physical	26186194
DCAM_HUMAN	AMD1	physical	26186194
RECQ5_HUMAN	RECQL5	physical	26186194
RPB2_HUMAN	POLR2B	physical	26186194
SHIP2_HUMAN	INPPL1	physical	26186194
COA1_HUMAN	COA1	physical	26186194
SPT6H_HUMAN	SUPT6H	physical	26186194
GPN1_HUMAN	GPN1	physical	26186194
RPB11_HUMAN	POLR2J	physical	26186194
UBR2_HUMAN	UBR2	physical	26186194
RPB9_HUMAN	POLR2I	physical	26186194
RPAB1_HUMAN	POLR2E	physical	26186194
RPB3_HUMAN	POLR2C	physical	26186194
BIN1_HUMAN	BIN1	physical	26186194
SSNA1_HUMAN	SSNA1	physical	26186194
KLH26_HUMAN	KLHL26	physical	26186194
FRIL_HUMAN	FTL	physical	26186194
FABD_HUMAN	MCAT	physical	26186194
RPAB5_HUMAN	POLR2L	physical	26186194
GPN2_HUMAN	GPN2	physical	26186194
RPAB2_HUMAN	POLR2F	physical	26186194
RPB7_HUMAN	POLR2G	physical	28514442
RECQ5_HUMAN	RECQL5	physical	28514442
BIN1_HUMAN	BIN1	physical	28514442
RPR1A_HUMAN	RPRD1A	physical	28514442
RPAP2_HUMAN	RPAP2	physical	28514442
GPN2_HUMAN	GPN2	physical	28514442
COA1_HUMAN	COA1	physical	28514442
SPT6H_HUMAN	SUPT6H	physical	28514442
UBP47_HUMAN	USP47	physical	28514442
RPB1_HUMAN	POLR2A	physical	28514442
RPB9_HUMAN	POLR2I	physical	28514442
RPB11_HUMAN	POLR2J	physical	28514442
RPAP1_HUMAN	RPAP1	physical	28514442
GPN1_HUMAN	GPN1	physical	28514442
DCAM_HUMAN	AMD1	physical	28514442
RPB3_HUMAN	POLR2C	physical	28514442
RPAB5_HUMAN	POLR2L	physical	28514442
RPB2_HUMAN	POLR2B	physical	28514442
SHIP2_HUMAN	INPPL1	physical	28514442
KLH26_HUMAN	KLHL26	physical	28514442
SSNA1_HUMAN	SSNA1	physical	28514442
RPAB2_HUMAN	POLR2F	physical	28514442
FRIL_HUMAN	FTL	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 GRL1A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-185 AND SER-270, ANDMASS SPECTROMETRY.	18669648 [Abstract]