dbPTM

H12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H12_HUMAN
UniProt AC	P16403
Protein Name	Histone H1.2
Gene Name	HIST1H1C
Organism	Homo sapiens (Human).
Sequence Length	213
Subcellular Localization	Nucleus. Chromosome. Mainly localizes in euchromatin. Distribution goes in parallel with DNA concentration.
Protein Description	Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity)..
Protein Sequence	MSETAPAAPAAAPPAEKAPVKKKAAKKAGGTPRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKVKKAGGTKPKKPVGAAKKPKKAAGGATPKKSAKKTPKKAKKPAAATVTKKVAKSPKKAKVAKPKKAAKSAAKAVKPKAAKPKVVKPKKAAPKKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSETAPAAP ------CCCCCCCCC	43.59	19691289
2	Phosphorylation	------MSETAPAAP ------CCCCCCCCC	43.59	29255136
4	Phosphorylation	----MSETAPAAPAA ----CCCCCCCCCCC	30.54	29255136
17	Acetylation	AAAPPAEKAPVKKKA CCCCCHHHCCCCHHH	61.16	23749302
17	Ubiquitination	AAAPPAEKAPVKKKA CCCCCHHHCCCCHHH	61.16	23000965
21	Glycation	PAEKAPVKKKAAKKA CHHHCCCCHHHHHHC	47.71	-
21	Ubiquitination	PAEKAPVKKKAAKKA CHHHCCCCHHHHHHC	47.71	23000965
22	Glycation	AEKAPVKKKAAKKAG HHHCCCCHHHHHHCC	48.13	-
22	Ubiquitination	AEKAPVKKKAAKKAG HHHCCCCHHHHHHCC	48.13	23000965
23	Glycation	EKAPVKKKAAKKAGG HHCCCCHHHHHHCCC	48.11	-
23	Other	EKAPVKKKAAKKAGG HHCCCCHHHHHHCCC	48.11	24681537
23	Ubiquitination	EKAPVKKKAAKKAGG HHCCCCHHHHHHCCC	48.11	23000965
26	Acetylation	PVKKKAAKKAGGTPR CCCHHHHHHCCCCCC	48.27	-
26	Methylation	PVKKKAAKKAGGTPR CCCHHHHHHCCCCCC	48.27	17043054
26	Other	PVKKKAAKKAGGTPR CCCHHHHHHCCCCCC	48.27	24681537
27	Glycation	VKKKAAKKAGGTPRK CCHHHHHHCCCCCCC	47.76	-
27	Lactylation	VKKKAAKKAGGTPRK CCHHHHHHCCCCCCC	47.76	31645732
27	Other	VKKKAAKKAGGTPRK CCHHHHHHCCCCCCC	47.76	24681537
31	Phosphorylation	AAKKAGGTPRKASGP HHHHCCCCCCCCCCC	20.99	26329039
34	N6-crotonyl-L-lysine	KAGGTPRKASGPPVS HCCCCCCCCCCCCHH	48.37	-
34	Acetylation	KAGGTPRKASGPPVS HCCCCCCCCCCCCHH	48.37	17043054
34	Crotonylation	KAGGTPRKASGPPVS HCCCCCCCCCCCCHH	48.37	21925322
34	Malonylation	KAGGTPRKASGPPVS HCCCCCCCCCCCCHH	48.37	26320211
34	Methylation	KAGGTPRKASGPPVS HCCCCCCCCCCCCHH	48.37	17043054
34	Other	KAGGTPRKASGPPVS HCCCCCCCCCCCCHH	48.37	-
34	Ubiquitination	KAGGTPRKASGPPVS HCCCCCCCCCCCCHH	48.37	23000965
36	Phosphorylation	GGTPRKASGPPVSEL CCCCCCCCCCCHHHH	55.67	29255136
41	Phosphorylation	KASGPPVSELITKAV CCCCCCHHHHHHHHH	32.24	30266825
45	Phosphorylation	PPVSELITKAVAASK CCHHHHHHHHHHHHH	26.10	30266825
46	Ubiquitination	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	21890473
46	Acetylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	22641341
46	Malonylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	26320211
46	Methylation	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	17043054
46	Other	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	24681537
46	Ubiquitination	PVSELITKAVAASKE CHHHHHHHHHHHHHH	33.59	25015289
51	Phosphorylation	ITKAVAASKERSGVS HHHHHHHHHHCCCCC	25.88	26546556
52	Acetylation	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	7296767
52	Lactylation	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	31645732
52	Methylation	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	17043054
52	Other	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	24681537
52	Ubiquitination	TKAVAASKERSGVSL HHHHHHHHHCCCCCH	53.04	23000965
54	Citrullination	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
54	Citrullination	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
54	Methylation	AVAASKERSGVSLAA HHHHHHHCCCCCHHH	42.31	-
55	Phosphorylation	VAASKERSGVSLAAL HHHHHHCCCCCHHHH	44.64	30266825
58	Phosphorylation	SKERSGVSLAALKKA HHHCCCCCHHHHHHH	18.80	30266825
63	Acetylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	163891
63	Malonylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	26320211
63	Methylation	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	17043054
63	Other	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	24681537
63	Ubiquitination	GVSLAALKKALAAAG CCCHHHHHHHHHHCC	31.13	23000965
64	Ubiquitination	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	21890473
64	N6-crotonyl-L-lysine	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	-
64	Acetylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	17043054
64	Crotonylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	21925322
64	Malonylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	26320211
64	Other	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	24681537
64	Sumoylation	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	17043054
64	Ubiquitination	VSLAALKKALAAAGY CCHHHHHHHHHHCCC	49.86	23000965
71	Phosphorylation	KALAAAGYDVEKNNS HHHHHCCCCCHHCCC	16.46	28152594
75	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	21890473
75	Acetylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	158559
75	Malonylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	26320211
75	Methylation	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	-
75	Other	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	24681537
75	Ubiquitination	AAGYDVEKNNSRIKL HCCCCCHHCCCCCCC	62.37	23000965
78	Phosphorylation	YDVEKNNSRIKLGLK CCCHHCCCCCCCCHH	44.79	23401153
81	Other	EKNNSRIKLGLKSLV HHCCCCCCCCHHHHH	35.08	24681537
81	Ubiquitination	EKNNSRIKLGLKSLV HHCCCCCCCCHHHHH	35.08	23000965
85	Ubiquitination	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	21890473
85	N6-crotonyl-L-lysine	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	-
85	Acetylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	72630437
85	Crotonylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	21925322
85	Malonylation	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	26320211
85	Other	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	24681537
85	Ubiquitination	SRIKLGLKSLVSKGT CCCCCCHHHHHHCCC	39.69	23000965
86	Phosphorylation	RIKLGLKSLVSKGTL CCCCCHHHHHHCCCE	38.76	20860994
89	Phosphorylation	LGLKSLVSKGTLVQT CCHHHHHHCCCEEEE	30.57	17877366
90	Ubiquitination	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	21890473
90	N6-crotonyl-L-lysine	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	-
90	Acetylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	17043054
90	Crotonylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	21925322
90	Lactylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	31645732
90	Malonylation	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	26320211
90	Other	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	24681537
90	Ubiquitination	GLKSLVSKGTLVQTK CHHHHHHCCCEEEEC	48.73	23000965
92	Phosphorylation	KSLVSKGTLVQTKGT HHHHHCCCEEEECCC	27.74	17877366
96	Phosphorylation	SKGTLVQTKGTGASG HCCCEEEECCCCCCC	24.78	28111955
97	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	21890473
97	N6-crotonyl-L-lysine	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
97	Acetylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	17043054
97	Crotonylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	21925322
97	Lactylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	31645732
97	Malonylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	26320211
97	Other	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	24681537
97	Succinylation	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	-
97	Ubiquitination	KGTLVQTKGTGASGS CCCEEEECCCCCCCC	37.07	23000965
99	Phosphorylation	TLVQTKGTGASGSFK CEEEECCCCCCCCEE	31.00	26657352
102	Phosphorylation	QTKGTGASGSFKLNK EECCCCCCCCEECCC	35.99	25159151
104	Phosphorylation	KGTGASGSFKLNKKA CCCCCCCCEECCCCC	19.40	23401153
106	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	21890473
106	Acetylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	22641351
106	Malonylation	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	26320211
106	Other	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	-
106	Ubiquitination	TGASGSFKLNKKAAS CCCCCCEECCCCCCC	53.50	21906983
109	Ubiquitination	SGSFKLNKKAASGEA CCCEECCCCCCCCCC	54.98	22817900
110	Other	GSFKLNKKAASGEAK CCEECCCCCCCCCCC	48.38	24681537
110	Ubiquitination	GSFKLNKKAASGEAK CCEECCCCCCCCCCC	48.38	21906983
113	Phosphorylation	KLNKKAASGEAKPKV ECCCCCCCCCCCCCC	41.86	26657352
117	Acetylation	KAASGEAKPKVKKAG CCCCCCCCCCCCCCC	40.86	26051181
117	Other	KAASGEAKPKVKKAG CCCCCCCCCCCCCCC	40.86	24681537
117	Ubiquitination	KAASGEAKPKVKKAG CCCCCCCCCCCCCCC	40.86	21906983
119	Methylation	ASGEAKPKVKKAGGT CCCCCCCCCCCCCCC	67.01	-
119	Ubiquitination	ASGEAKPKVKKAGGT CCCCCCCCCCCCCCC	67.01	22817900
121	Other	GEAKPKVKKAGGTKP CCCCCCCCCCCCCCC	42.93	24681537
121	Ubiquitination	GEAKPKVKKAGGTKP CCCCCCCCCCCCCCC	42.93	22817900
122	Ubiquitination	EAKPKVKKAGGTKPK CCCCCCCCCCCCCCC	56.08	22817900
126	Phosphorylation	KVKKAGGTKPKKPVG CCCCCCCCCCCCCCC	43.16	-
127	Ubiquitination	VKKAGGTKPKKPVGA CCCCCCCCCCCCCCC	59.10	21906983
129	Other	KAGGTKPKKPVGAAK CCCCCCCCCCCCCCC	71.86	24681537
129	Ubiquitination	KAGGTKPKKPVGAAK CCCCCCCCCCCCCCC	71.86	22817900
130	Ubiquitination	AGGTKPKKPVGAAKK CCCCCCCCCCCCCCC	54.16	22817900
136	Glycation	KKPVGAAKKPKKAAG CCCCCCCCCCCCCCC	69.90	-
136	Other	KKPVGAAKKPKKAAG CCCCCCCCCCCCCCC	69.90	24681537
136	Ubiquitination	KKPVGAAKKPKKAAG CCCCCCCCCCCCCCC	69.90	22817900
137	Ubiquitination	KPVGAAKKPKKAAGG CCCCCCCCCCCCCCC	58.29	22817900
139	Ubiquitination	VGAAKKPKKAAGGAT CCCCCCCCCCCCCCC	65.02	22817900
140	Lactylation	GAAKKPKKAAGGATP CCCCCCCCCCCCCCC	52.58	31645732
140	Ubiquitination	GAAKKPKKAAGGATP CCCCCCCCCCCCCCC	52.58	21906983
146	Phosphorylation	KKAAGGATPKKSAKK CCCCCCCCCCCCCCC	38.63	30266825
148	Other	AAGGATPKKSAKKTP CCCCCCCCCCCCCCC	55.81	24681537
148	Ubiquitination	AAGGATPKKSAKKTP CCCCCCCCCCCCCCC	55.81	33845483
153	Ubiquitination	TPKKSAKKTPKKAKK CCCCCCCCCCCCCCC	70.54	23503661
154	Phosphorylation	PKKSAKKTPKKAKKP CCCCCCCCCCCCCCC	39.37	-
156	Ubiquitination	KSAKKTPKKAKKPAA CCCCCCCCCCCCCCH	71.27	22817900
157	Acetylation	SAKKTPKKAKKPAAA CCCCCCCCCCCCCHH	67.64	7429635
157	Glycation	SAKKTPKKAKKPAAA CCCCCCCCCCCCCHH	67.64	-
157	Ubiquitination	SAKKTPKKAKKPAAA CCCCCCCCCCCCCHH	67.64	22817900
159	N6-crotonyl-L-lysine	KKTPKKAKKPAAATV CCCCCCCCCCCHHHH	69.07	-
159	Acetylation	KKTPKKAKKPAAATV CCCCCCCCCCCHHHH	69.07	26051181
159	Crotonylation	KKTPKKAKKPAAATV CCCCCCCCCCCHHHH	69.07	21925322
159	Other	KKTPKKAKKPAAATV CCCCCCCCCCCHHHH	69.07	24681537
159	Ubiquitination	KKTPKKAKKPAAATV CCCCCCCCCCCHHHH	69.07	22817900
160	Acetylation	KTPKKAKKPAAATVT CCCCCCCCCCHHHHH	44.76	7429651
160	Ubiquitination	KTPKKAKKPAAATVT CCCCCCCCCCHHHHH	44.76	21906983
165	Phosphorylation	AKKPAAATVTKKVAK CCCCCHHHHHHHHHC	24.79	30266825
167	Phosphorylation	KPAAATVTKKVAKSP CCCHHHHHHHHHCCC	22.31	30266825
168	N6-crotonyl-L-lysine	PAAATVTKKVAKSPK CCHHHHHHHHHCCCC	40.70	-
168	Acetylation	PAAATVTKKVAKSPK CCHHHHHHHHHCCCC	40.70	17043054
168	Crotonylation	PAAATVTKKVAKSPK CCHHHHHHHHHCCCC	40.70	21925322
168	Lactylation	PAAATVTKKVAKSPK CCHHHHHHHHHCCCC	40.70	31645732
168	Methylation	PAAATVTKKVAKSPK CCHHHHHHHHHCCCC	40.70	-
168	Other	PAAATVTKKVAKSPK CCHHHHHHHHHCCCC	40.70	24681537
168	Ubiquitination	PAAATVTKKVAKSPK CCHHHHHHHHHCCCC	40.70	27667366
169	Acetylation	AAATVTKKVAKSPKK CHHHHHHHHHCCCCC	37.75	164213
169	Ubiquitination	AAATVTKKVAKSPKK CHHHHHHHHHCCCCC	37.75	22817900
172	Glycation	TVTKKVAKSPKKAKV HHHHHHHCCCCCCCC	70.99	-
172	Ubiquitination	TVTKKVAKSPKKAKV HHHHHHHCCCCCCCC	70.99	22817900
173	Phosphorylation	VTKKVAKSPKKAKVA HHHHHHCCCCCCCCC	32.01	30278072
175	Glycation	KKVAKSPKKAKVAKP HHHHCCCCCCCCCCH	72.89	-
178	Ubiquitination	AKSPKKAKVAKPKKA HCCCCCCCCCCHHHH	52.16	-
187	"N6,N6-dimethyllysine"	AKPKKAAKSAAKAVK CCHHHHHHHHHHHHC	45.55	-
187	Acetylation	AKPKKAAKSAAKAVK CCHHHHHHHHHHHHC	45.55	7704193
187	Methylation	AKPKKAAKSAAKAVK CCHHHHHHHHHHHHC	45.55	20334638
188	ADP-ribosylation	KPKKAAKSAAKAVKP CHHHHHHHHHHHHCC	28.82	27723750
188	Phosphorylation	KPKKAAKSAAKAVKP CHHHHHHHHHHHHCC	28.82	-
191	Acetylation	KAAKSAAKAVKPKAA HHHHHHHHHHCCCCC	54.12	17043054
191	Lactylation	KAAKSAAKAVKPKAA HHHHHHHHHHCCCCC	54.12	31645732
191	Ubiquitination	KAAKSAAKAVKPKAA HHHHHHHHHHCCCCC	54.12	33845483
194	Ubiquitination	KSAAKAVKPKAAKPK HHHHHHHCCCCCCCC	45.73	25015289
196	Ubiquitination	AAKAVKPKAAKPKVV HHHHHCCCCCCCCCC	56.08	25015289
199	Glycation	AVKPKAAKPKVVKPK HHCCCCCCCCCCCCC	50.67	-
199	Ubiquitination	AVKPKAAKPKVVKPK HHCCCCCCCCCCCCC	50.67	25015289
201	Glycation	KPKAAKPKVVKPKKA CCCCCCCCCCCCCCC	59.98	-
201	Lactylation	KPKAAKPKVVKPKKA CCCCCCCCCCCCCCC	59.98	31645732
201	Ubiquitination	KPKAAKPKVVKPKKA CCCCCCCCCCCCCCC	59.98	22817900
204	Ubiquitination	AAKPKVVKPKKAAPK CCCCCCCCCCCCCCC	54.85	22817900
206	Ubiquitination	KPKVVKPKKAAPKKK CCCCCCCCCCCCCCC	49.69	22817900
207	Ubiquitination	PKVVKPKKAAPKKK- CCCCCCCCCCCCCC-	59.30	22817900
211	Ubiquitination	KPKKAAPKKK----- CCCCCCCCCC-----	69.35	22817900
213	Other	KKAAPKKK------- CCCCCCCC-------	72.24	24681537

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
36	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
55	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
89	S	Phosphorylation	Kinase	CHEK2	O96017	GPS
92	T	Phosphorylation	Kinase	CHEK2	O96017	GPS
104	S	Phosphorylation	Kinase	PKC	-	Uniprot
146	T	Phosphorylation	Kinase	PRKDC	P78527	GPS
167	T	Phosphorylation	Kinase	CHEK2	O96017	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:30517763

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
54	R	Citrullination		-
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.

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 H12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUZ12_HUMAN	SUZ12	physical	16431907
EED_HUMAN	EED	physical	16431907
AEBP2_HUMAN	AEBP2	physical	16431907
PRKDC_HUMAN	PRKDC	physical	18258596
ASXL1_HUMAN	ASXL1	physical	18258596
PARP1_HUMAN	PARP1	physical	18258596
IMA8_HUMAN	KPNA7	physical	18258596
NUCL_HUMAN	NCL	physical	18258596
CTNB1_HUMAN	CTNNB1	physical	18258596
IMB1_HUMAN	KPNB1	physical	18258596
WDR5_HUMAN	WDR5	physical	18258596
WDR12_HUMAN	WDR12	physical	18258596
RBM39_HUMAN	RBM39	physical	18258596
YBOX1_HUMAN	YBX1	physical	18258596
PUF60_HUMAN	PUF60	physical	18258596
H1X_HUMAN	H1FX	physical	22939629
H2A1D_HUMAN	HIST1H2AD	physical	22939629
IL7RA_HUMAN	IL7R	physical	23151878
SC24D_HUMAN	SEC24D	physical	22863883
CUL4A_HUMAN	CUL4A	physical	24360965
PAF1_HUMAN	PAF1	physical	24360965
LEO1_HUMAN	LEO1	physical	24360965
RPB1_HUMAN	POLR2A	physical	24360965
CTR9_HUMAN	CTR9	physical	24360965
CDC73_HUMAN	CDC73	physical	24360965
WDR61_HUMAN	WDR61	physical	24360965
DDB1_HUMAN	DDB1	physical	24360965
RBX1_HUMAN	RBX1	physical	24360965
WDR5_HUMAN	WDR5	physical	24360965
DCAF1_HUMAN	VPRBP	physical	24360965
FIP1_HUMAN	FIP1L1	physical	26344197

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 H12_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, UBIQUITINATION [LARGESCALE ANALYSIS] AT LYS-17, AND MASS SPECTROMETRY.	18781797 [Abstract]
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-36, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-2 AND THR-4, AND MASSSPECTROMETRY.	19413330 [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-36, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-36 AND THR-146,AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-36, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-173, AND MASSSPECTROMETRY.	17081983 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, UBIQUITINATION [LARGESCALE ANALYSIS] AT LYS-17, AND MASS SPECTROMETRY.	18781797 [Abstract]
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206, AND MASSSPECTROMETRY.	17370265 [Abstract]

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