DPOLM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPOLM_HUMAN
• UniProt AC: Q9NP87
• Protein Name: DNA-directed DNA/RNA polymerase mu
• Gene Name: POLM
• Organism: Homo sapiens (Human).
• Sequence Length: 494
• Subcellular Localization: Nucleus.
• Protein Description: Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination..
• Protein Sequence: MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECRHRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLILYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFRHLGLEYLPPEQRNA

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
12	Phosphorylation	RRRARVGSPSGDAAS CCCCCCCCCCCCHHC	17.03	19664994
14	Phosphorylation	RARVGSPSGDAASST CCCCCCCCCCHHCCC	51.51	30266825
19	Phosphorylation	SPSGDAASSTPPSTR CCCCCHHCCCCCCCC	36.14	23927012
20	Phosphorylation	PSGDAASSTPPSTRF CCCCHHCCCCCCCCC	39.96	23927012
21	Phosphorylation	SGDAASSTPPSTRFP CCCHHCCCCCCCCCC	36.40	23927012
24	Phosphorylation	AASSTPPSTRFPGVA HHCCCCCCCCCCCEE	33.16	23927012
25	Phosphorylation	ASSTPPSTRFPGVAI HCCCCCCCCCCCEEE	41.94	23927012
33	Phosphorylation	RFPGVAIYLVEPRMG CCCCEEEEEECCCCC	8.58	26074081
48	Phosphorylation	RSRRAFLTGLARSKG CCHHHHHHHHHHCCC	24.56	23403867
53	Phosphorylation	FLTGLARSKGFRVLD HHHHHHHCCCCCHHH	31.36	23403867
95	Phosphorylation	AAAPPGCTPPALLDI HCCCCCCCCHHHHCH	37.92	-
178	Phosphorylation	GSEGRLLTFCRAASV CCHHHHHHHHHHHHH	25.86	29507054
184	Phosphorylation	LTFCRAASVLKALPS HHHHHHHHHHHHCCC	27.31	29507054
187	Ubiquitination	CRAASVLKALPSPVT HHHHHHHHHCCCCCC	45.80	-
238	Ubiquitination	SERYQTMKLFTQIFG HHHHHHHHHHHHHHC	43.78	-
249	Ubiquitination	QIFGVGVKTADRWYR HHHCCCHHHHHHHHH	31.87	-
271	Ubiquitination	DLREQPQKLTQQQKA HHHHCHHHHHHHHHH	61.25	29967540
277	Ubiquitination	QKLTQQQKAGLQHHQ HHHHHHHHHHHHHCH	39.83	-
277	Ubiquitination	QKLTQQQKAGLQHHQ HHHHHHHHHHHHHCH	39.83	29967540
325	Ubiquitination	TGGFRRGKLQGHDVD ECCCCCCCCCCCEEC	35.51	-
339	Ubiquitination	DFLITHPKEGQEAGL CEEEECCCCCHHCCC	67.86	-
362	Phosphorylation	QDQGLILYHQHQHSC HHCCEEEEEECCCCC	7.76	23312004
368	Phosphorylation	LYHQHQHSCCESPTR EEEECCCCCCCCHHH	17.56	23312004
372	Phosphorylation	HQHSCCESPTRLAQQ CCCCCCCCHHHHHHH	20.05	28464451
372	Ubiquitination	HQHSCCESPTRLAQQ CCCCCCCCHHHHHHH	20.05	29967540
374	Phosphorylation	HSCCESPTRLAQQSH CCCCCCHHHHHHHHC	47.82	23312004
392	Ubiquitination	FERSFCIFRLPQPPG HHCCEEEEECCCCCC	7.45	-
414	Ubiquitination	RPCPSWKAVRVDLVV CCCCCCCEEEEEEEE	6.52	-
415	Ubiquitination	PCPSWKAVRVDLVVA CCCCCCEEEEEEEEE	5.64	-
415	Ubiquitination	PCPSWKAVRVDLVVA CCCCCCEEEEEEEEE	5.64	29967540
430	Ubiquitination	PVSQFPFALLGWTGS EHHHCCHHHHCCCCH	11.34	29967540
452	Ubiquitination	RRFSRKEKGLWLNSH HHHHHHHCCEEECCC	63.44	29967540
467	Ubiquitination	GLFDPEQKTFFQAAS CCCCHHHHHHHHHCC	45.71	29967540

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
372	S	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPOLM_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 DPOLM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CEP55_HUMAN	CEP55	physical	25416956
CTU2_HUMAN	CTU2	physical	28514442
ACAD8_HUMAN	ACAD8	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-12, AND MASSSPECTROMETRY.
PubMed: 19690332

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-12, AND MASSSPECTROMETRY.
PubMed: 18669648