dbPTM

HNRPD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HNRPD_HUMAN
UniProt AC	Q14103
Protein Name	Heterogeneous nuclear ribonucleoprotein D0
Gene Name	HNRNPD
Organism	Homo sapiens (Human).
Sequence Length	355
Subcellular Localization	Nucleus. Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally.
Protein Description	Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation..
Protein Sequence	MSEEQFGGDGAAAAATAAVGGSAGEQEGAMVAATQGAAAAAGSGAGTGGGTASGGTEGGSAESEGAKIDASKNEEDEGHSNSSPRHSEAATAQREEWKMFIGGLSWDTTKKDLKDYFSKFGEVVDCTLKLDPITGRSRGFGFVLFKESESVDKVMDQKEHKLNGKVIDPKRAKAMKTKEPVKKIFVGGLSPDTPEEKIREYFGGFGEVESIELPMDNKTNKRRGFCFITFKEEEPVKKIMEKKYHNVGLSKCEIKVAMSKEQYQQQQQWGSRGGFAGRARGRGGGPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSNQQSGYGKVSRRGGHQNSYKPY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSEEQFGGD ------CCHHHCCCH	50.25	19413330
2	Phosphorylation	------MSEEQFGGD ------CCHHHCCCH	50.25	19413330
16	Phosphorylation	DGAAAAATAAVGGSA HHHHHHHHHHHCCCH	15.49	27251275
22	Phosphorylation	ATAAVGGSAGEQEGA HHHHHCCCHHHHHHH	27.46	21601212
34	Phosphorylation	EGAMVAATQGAAAAA HHHHEHHHCHHHHHC	20.14	27251275
43	Phosphorylation	GAAAAAGSGAGTGGG HHHHHCCCCCCCCCC	22.27	27251275
47	Phosphorylation	AAGSGAGTGGGTASG HCCCCCCCCCCCCCC	31.92	27251275
51	Phosphorylation	GAGTGGGTASGGTEG CCCCCCCCCCCCCCC	22.41	27251275
56	Phosphorylation	GGTASGGTEGGSAES CCCCCCCCCCCCCCC	34.68	24505115
60	Phosphorylation	SGGTEGGSAESEGAK CCCCCCCCCCCCCCC	39.45	22817901
63	Phosphorylation	TEGGSAESEGAKIDA CCCCCCCCCCCCCCC	40.84	22817901
71	Phosphorylation	EGAKIDASKNEEDEG CCCCCCCCCCCCCCC	32.06	29255136
72	Acetylation	GAKIDASKNEEDEGH CCCCCCCCCCCCCCC	70.83	23749302
72	Ubiquitination	GAKIDASKNEEDEGH CCCCCCCCCCCCCCC	70.83	21906983
72	Sumoylation	GAKIDASKNEEDEGH CCCCCCCCCCCCCCC	70.83	28112733
72 (in isoform 1)	Ubiquitination	-	70.83	21890473
72 (in isoform 3)	Ubiquitination	-	70.83	21890473
80	Phosphorylation	NEEDEGHSNSSPRHS CCCCCCCCCCCHHHH	49.62	29255136
82	Phosphorylation	EDEGHSNSSPRHSEA CCCCCCCCCHHHHHH	44.74	29255136
83	Phosphorylation	DEGHSNSSPRHSEAA CCCCCCCCHHHHHHH	30.15	29255136
87	Phosphorylation	SNSSPRHSEAATAQR CCCCHHHHHHHHHCH	30.15	29255136
91	Phosphorylation	PRHSEAATAQREEWK HHHHHHHHHCHHHHH	30.30	30266825
91 (in isoform 2)	Ubiquitination	-	30.30	21890473
91 (in isoform 4)	Ubiquitination	-	30.30	21890473
94	Methylation	SEAATAQREEWKMFI HHHHHHCHHHHHHHH	41.14	115386471
95 (in isoform 2)	Ubiquitination	-	57.01	21890473
95 (in isoform 4)	Ubiquitination	-	57.01	21890473
98	Acetylation	TAQREEWKMFIGGLS HHCHHHHHHHHCCCC	27.49	25953088
99	Sulfoxidation	AQREEWKMFIGGLSW HCHHHHHHHHCCCCC	2.87	28183972
100 (in isoform 2)	Ubiquitination	-	4.10	21890473
100 (in isoform 4)	Ubiquitination	-	4.10	21890473
105	Phosphorylation	KMFIGGLSWDTTKKD HHHHCCCCCCCCHHH	26.61	-
108	Phosphorylation	IGGLSWDTTKKDLKD HCCCCCCCCHHHHHH	33.97	19664994
110	Acetylation	GLSWDTTKKDLKDYF CCCCCCCHHHHHHHH	46.51	26051181
110	Ubiquitination	GLSWDTTKKDLKDYF CCCCCCCHHHHHHHH	46.51	21906983
110 (in isoform 3)	Ubiquitination	-	46.51	21890473
110 (in isoform 1)	Ubiquitination	-	46.51	21890473
110 (in isoform 2)	Ubiquitination	-	46.51	21890473
110 (in isoform 4)	Ubiquitination	-	46.51	21890473
111	Acetylation	LSWDTTKKDLKDYFS CCCCCCHHHHHHHHH	67.22	24469531
111	Ubiquitination	LSWDTTKKDLKDYFS CCCCCCHHHHHHHHH	67.22	-
111 (in isoform 3)	Ubiquitination	-	67.22	-
111	Malonylation	LSWDTTKKDLKDYFS CCCCCCHHHHHHHHH	67.22	26320211
114	Acetylation	DTTKKDLKDYFSKFG CCCHHHHHHHHHHHC	61.59	25825284
114	Ubiquitination	DTTKKDLKDYFSKFG CCCHHHHHHHHHHHC	61.59	21890473
114 (in isoform 3)	Ubiquitination	-	61.59	21890473
114	Succinylation	DTTKKDLKDYFSKFG CCCHHHHHHHHHHHC	61.59	23954790
114 (in isoform 1)	Ubiquitination	-	61.59	21890473
116	Phosphorylation	TKKDLKDYFSKFGEV CHHHHHHHHHHHCCE	14.25	28152594
118	Phosphorylation	KDLKDYFSKFGEVVD HHHHHHHHHHCCEEE	22.35	28152594
119	Acetylation	DLKDYFSKFGEVVDC HHHHHHHHHCCEEEE	47.71	25825284
119	Methylation	DLKDYFSKFGEVVDC HHHHHHHHHCCEEEE	47.71	23161681
119	Ubiquitination	DLKDYFSKFGEVVDC HHHHHHHHHCCEEEE	47.71	21890473
119 (in isoform 3)	Ubiquitination	-	47.71	21890473
119 (in isoform 1)	Ubiquitination	-	47.71	21890473
126	S-nitrosocysteine	KFGEVVDCTLKLDPI HHCCEEEEEEEECCC	3.03	-
126	Glutathionylation	KFGEVVDCTLKLDPI HHCCEEEEEEEECCC	3.03	22555962
126	S-nitrosylation	KFGEVVDCTLKLDPI HHCCEEEEEEEECCC	3.03	19483679
127	Phosphorylation	FGEVVDCTLKLDPIT HCCEEEEEEEECCCC	23.59	19664994
129	Acetylation	EVVDCTLKLDPITGR CEEEEEEEECCCCCC	32.46	23749302
129	Ubiquitination	EVVDCTLKLDPITGR CEEEEEEEECCCCCC	32.46	22053931
129 (in isoform 3)	Ubiquitination	-	32.46	21890473
129	Methylation	EVVDCTLKLDPITGR CEEEEEEEECCCCCC	32.46	23583077
129	Sumoylation	EVVDCTLKLDPITGR CEEEEEEEECCCCCC	32.46	28112733
129 (in isoform 1)	Ubiquitination	-	32.46	21890473
134	Phosphorylation	TLKLDPITGRSRGFG EEEECCCCCCCCCEE	31.75	23403867
137	Phosphorylation	LDPITGRSRGFGFVL ECCCCCCCCCEEEEE	37.79	24719451
138	Methylation	DPITGRSRGFGFVLF CCCCCCCCCEEEEEE	43.00	-
146	Acetylation	GFGFVLFKESESVDK CEEEEEEECCCCHHH	57.05	19608861
153	Acetylation	KESESVDKVMDQKEH ECCCCHHHHHHHHHH	36.99	23749302
153	Ubiquitination	KESESVDKVMDQKEH ECCCCHHHHHHHHHH	36.99	-
153 (in isoform 3)	Ubiquitination	-	36.99	-
155	Sulfoxidation	SESVDKVMDQKEHKL CCCHHHHHHHHHHHH	5.79	21406390
158	Acetylation	VDKVMDQKEHKLNGK HHHHHHHHHHHHCCE	58.48	25953088
161 (in isoform 3)	Ubiquitination	-	44.75	-
164 (in isoform 2)	Ubiquitination	-	35.72	21890473
164 (in isoform 4)	Ubiquitination	-	35.72	21890473
165	Acetylation	KEHKLNGKVIDPKRA HHHHHCCEECCHHHH	34.64	19608861
165	Ubiquitination	KEHKLNGKVIDPKRA HHHHHCCEECCHHHH	34.64	19608861
165 (in isoform 3)	Ubiquitination	-	34.64	-
170	Ubiquitination	NGKVIDPKRAKAMKT CCEECCHHHHHHCCC	62.33	-
178 (in isoform 2)	Ubiquitination	-	55.28	21890473
178 (in isoform 4)	Ubiquitination	-	55.28	21890473
183	Ubiquitination	KTKEPVKKIFVGGLS CCCCCCCEEECCCCC	41.43	21890473
183	Malonylation	KTKEPVKKIFVGGLS CCCCCCCEEECCCCC	41.43	26320211
183	Acetylation	KTKEPVKKIFVGGLS CCCCCCCEEECCCCC	41.43	26051181
183 (in isoform 1)	Ubiquitination	-	41.43	21890473
183 (in isoform 3)	Ubiquitination	-	41.43	21890473
190	Phosphorylation	KIFVGGLSPDTPEEK EEECCCCCCCCHHHH	24.81	19664994
193	Phosphorylation	VGGLSPDTPEEKIRE CCCCCCCCHHHHHHH	35.66	29255136
197	Acetylation	SPDTPEEKIREYFGG CCCCHHHHHHHHHCC	45.46	23954790
197	Ubiquitination	SPDTPEEKIREYFGG CCCCHHHHHHHHHCC	45.46	21890473
197	Sumoylation	SPDTPEEKIREYFGG CCCCHHHHHHHHHCC	45.46	28112733
197 (in isoform 3)	Ubiquitination	-	45.46	21890473
197	Malonylation	SPDTPEEKIREYFGG CCCCHHHHHHHHHCC	45.46	26320211
197 (in isoform 1)	Ubiquitination	-	45.46	21890473
199 (in isoform 2)	Ubiquitination	-	43.56	21890473
199 (in isoform 4)	Ubiquitination	-	43.56	21890473
201	Phosphorylation	PEEKIREYFGGFGEV HHHHHHHHHCCCCCE	9.55	27642862
210	Phosphorylation	GGFGEVESIELPMDN CCCCCEEEEEECCCC	26.91	27732954
215	Sulfoxidation	VESIELPMDNKTNKR EEEEEECCCCCCCCC	16.14	30846556
218	Methylation	IELPMDNKTNKRRGF EEECCCCCCCCCCCE	49.57	66728815
218	Acetylation	IELPMDNKTNKRRGF EEECCCCCCCCCCCE	49.57	25953088
218	Ubiquitination	IELPMDNKTNKRRGF EEECCCCCCCCCCCE	49.57	21890473
218 (in isoform 3)	Ubiquitination	-	49.57	21890473
218 (in isoform 1)	Ubiquitination	-	49.57	21890473
224 (in isoform 2)	Ubiquitination	-	27.92	-
226	S-nitrosocysteine	TNKRRGFCFITFKEE CCCCCCEEEEEECCC	2.41	-
226	Glutathionylation	TNKRRGFCFITFKEE CCCCCCEEEEEECCC	2.41	22555962
226	S-nitrosylation	TNKRRGFCFITFKEE CCCCCCEEEEEECCC	2.41	19483679
231	Acetylation	GFCFITFKEEEPVKK CEEEEEECCCCHHHH	56.41	25825284
231	Ubiquitination	GFCFITFKEEEPVKK CEEEEEECCCCHHHH	56.41	-
232	Acetylation	FCFITFKEEEPVKKI EEEEEECCCCHHHHH	64.50	19608861
232	Ubiquitination	FCFITFKEEEPVKKI EEEEEECCCCHHHHH	64.50	19608861
237	Malonylation	FKEEEPVKKIMEKKY ECCCCHHHHHHHHHH	47.50	26320211
237	Acetylation	FKEEEPVKKIMEKKY ECCCCHHHHHHHHHH	47.50	25953088
238	Acetylation	KEEEPVKKIMEKKYH CCCCHHHHHHHHHHH	47.74	30583115
241 (in isoform 2)	Ubiquitination	-	50.28	-
243	Acetylation	VKKIMEKKYHNVGLS HHHHHHHHHHCCCCC	38.13	23749302
243	Ubiquitination	VKKIMEKKYHNVGLS HHHHHHHHHHCCCCC	38.13	-
244	Phosphorylation	KKIMEKKYHNVGLSK HHHHHHHHHCCCCCH	15.08	28152594
250	Phosphorylation	KYHNVGLSKCEIKVA HHHCCCCCHHEEEEE	29.36	24961811
251	Acetylation	YHNVGLSKCEIKVAM HHCCCCCHHEEEEEE	40.71	19608861
251	Ubiquitination	YHNVGLSKCEIKVAM HHCCCCCHHEEEEEE	40.71	19608861
251 (in isoform 3)	Ubiquitination	-	40.71	-
251	Malonylation	YHNVGLSKCEIKVAM HHCCCCCHHEEEEEE	40.71	26320211
255	Ubiquitination	GLSKCEIKVAMSKEQ CCCHHEEEEEECHHH	11.14	-
255	Acetylation	GLSKCEIKVAMSKEQ CCCHHEEEEEECHHH	11.14	25953088
260	Methylation	EIKVAMSKEQYQQQQ EEEEEECHHHHHHHH	35.43	115479067
260	Ubiquitination	EIKVAMSKEQYQQQQ EEEEEECHHHHHHHH	35.43	-
260 (in isoform 3)	Ubiquitination	-	35.43	-
263	Phosphorylation	VAMSKEQYQQQQQWG EEECHHHHHHHHHHH	14.91	23917254
263 (in isoform 4)	Methylation	-	14.91	24129315
269 (in isoform 4)	Phosphorylation	-	11.46	26434776
271	Phosphorylation	QQQQQWGSRGGFAGR HHHHHHHCCCCHHHC	25.45	23186163
271 (in isoform 4)	Phosphorylation	-	25.45	26434776
272	Dimethylation	QQQQWGSRGGFAGRA HHHHHHCCCCHHHCC	45.36	-
272	Methylation	QQQQWGSRGGFAGRA HHHHHHCCCCHHHCC	45.36	24129315
273 (in isoform 4)	Acetylation	-	36.95	19608861
273	Acetylation	QQQWGSRGGFAGRAR HHHHHCCCCHHHCCC	36.95	19608861
275 (in isoform 4)	Phosphorylation	-	7.89	26434776
277	Methylation	GSRGGFAGRARGRGG HCCCCHHHCCCCCCC	22.86	15782174
278	Dimethylation	SRGGFAGRARGRGGG CCCCHHHCCCCCCCC	20.06	-
278	Methylation	SRGGFAGRARGRGGG CCCCHHHCCCCCCCC	20.06	24129315
280	Dimethylation	GGFAGRARGRGGGPS CCHHHCCCCCCCCCC	33.70	-
280	Methylation	GGFAGRARGRGGGPS CCHHHCCCCCCCCCC	33.70	24129315
282	Dimethylation	FAGRARGRGGGPSQN HHHCCCCCCCCCCCC	34.72	-
282	Methylation	FAGRARGRGGGPSQN HHHCCCCCCCCCCCC	34.72	18583695
282 (in isoform 3)	Methylation	-	34.72	24129315
285	Acetylation	RARGRGGGPSQNWNQ CCCCCCCCCCCCCCC	22.85	19608861
288 (in isoform 3)	Phosphorylation	-	63.19	26434776
290 (in isoform 3)	Phosphorylation	-	7.29	26434776
292 (in isoform 3)	Ubiquitination	-	43.76	-
292 (in isoform 3)	Acetylation	-	43.76	19608861
294 (in isoform 3)	Phosphorylation	-	5.51	26434776
341	Acetylation	NQQSGYGKVSRRGGH CCCCCCCCCCCCCCC	28.67	26051181
343	Phosphorylation	QSGYGKVSRRGGHQN CCCCCCCCCCCCCCC	21.53	-
345	Asymmetric dimethylarginine	GYGKVSRRGGHQNSY CCCCCCCCCCCCCCC	48.19	-
345	Methylation	GYGKVSRRGGHQNSY CCCCCCCCCCCCCCC	48.19	24129315
351	Phosphorylation	RRGGHQNSYKPY--- CCCCCCCCCCCC---	28.15	26055452
353	Methylation	GGHQNSYKPY----- CCCCCCCCCC-----	37.35	19608861
353	Acetylation	GGHQNSYKPY----- CCCCCCCCCC-----	37.35	19608861

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
83	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
87	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
87	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
87	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
193	T	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	VHL	P40337	PMID:22086907
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:24658274

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
345	R	Methylation		15782174
Arg-345 is dimethylated, probably to asymmetric dimethylarginine.

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 HNRPD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LSM5_HUMAN	LSM5	physical	15231747
SAFB1_HUMAN	SAFB	physical	10933876
HSPB1_HUMAN	HSPB1	physical	18573886
HSP74_HUMAN	HSPA4	physical	18573886
HSP7C_HUMAN	HSPA8	physical	18573886
IF4G1_HUMAN	EIF4G1	physical	18573886
HNRPD_HUMAN	HNRNPD	physical	18573886
MTA2_HUMAN	MTA2	physical	18413351
HDAC1_HUMAN	HDAC1	physical	18413351
HSP74_HUMAN	HSPA4	physical	10205060
HSP7C_HUMAN	HSPA8	physical	10205060
IF4G1_HUMAN	EIF4G1	physical	10205060
PABP1_HUMAN	PABPC1	physical	10205060
HSPB1_HUMAN	HSPB1	physical	21245386
HSPB2_HUMAN	HSPB2	physical	21245386
HNRPD_HUMAN	HNRNPD	physical	21245386
HNRPD_HUMAN	HNRNPD	physical	12674497
HNRPQ_HUMAN	SYNCRIP	physical	12674497
YBOX1_HUMAN	YBX1	physical	12674497
IF2B2_HUMAN	IGF2BP2	physical	12674497
UBC9_HUMAN	UBE2I	physical	12674497
VHL_HUMAN	VHL	physical	22086907
VEGFA_HUMAN	VEGFA	physical	22086907
TNFA_HUMAN	TNF	physical	22086907
PABP1_HUMAN	PABPC1	physical	22939629
HNRPR_HUMAN	HNRNPR	physical	22939629
PTBP1_HUMAN	PTBP1	physical	22939629
RBMX_HUMAN	RBMX	physical	22939629
HNRPF_HUMAN	HNRNPF	physical	22939629
ROA1_HUMAN	HNRNPA1	physical	22939629
HNRPL_HUMAN	HNRNPL	physical	22939629
ROA2_HUMAN	HNRNPA2B1	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
ROA3_HUMAN	HNRNPA3	physical	22939629
RM12_HUMAN	MRPL12	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RALY_HUMAN	RALY	physical	22939629
RMD3_HUMAN	RMDN3	physical	22939629
SEPT9_HUMAN	SEPT9	physical	22939629
ZNT5_HUMAN	SLC30A5	physical	22939629
MSH2_HUMAN	MSH2	physical	22939629
HNRPD_HUMAN	HNRNPD	physical	16556936
IF4G1_HUMAN	EIF4G1	physical	16556936
PABP1_HUMAN	PABPC1	physical	16556936
HSP74_HUMAN	HSPA4	physical	16556936
1433S_HUMAN	SFN	physical	16902409
PABP1_HUMAN	PABPC1	physical	16902409
RU1C_HUMAN	SNRPC	physical	22365833
SF3B4_HUMAN	SF3B4	physical	22365833
U2AF2_HUMAN	U2AF2	physical	22365833
HNRPC_HUMAN	HNRNPC	physical	22365833
RALY_HUMAN	RALY	physical	22365833
HNRPU_HUMAN	HNRNPU	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
HNRPF_HUMAN	HNRNPF	physical	22365833
HNRH3_HUMAN	HNRNPH3	physical	22365833
PTBP1_HUMAN	PTBP1	physical	22365833
PTBP2_HUMAN	PTBP2	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
BRCA1_HUMAN	BRCA1	physical	22431556
HMGA1_HUMAN	HMGA1	physical	18850631
C1QBP_HUMAN	C1QBP	physical	15231747
RSSA_HUMAN	RPSA	physical	15231747
ACTB_HUMAN	ACTB	physical	15231747
TF3C3_HUMAN	GTF3C3	physical	15231747
CD97_HUMAN	CD97	physical	15231747
EXOS4_HUMAN	EXOSC4	physical	15231747
EF2_HUMAN	EEF2	physical	15231747
SNPC4_HUMAN	SNAPC4	physical	15231747
MRP7_HUMAN	ABCC10	physical	15231747
BET1L_HUMAN	BET1L	physical	15231747
SEN34_HUMAN	TSEN34	physical	15231747
CINP_HUMAN	CINP	physical	15231747
SHSA5_HUMAN	SHISA5	physical	15231747
EM55_HUMAN	MPP1	physical	15231747
DMAC1_HUMAN	TMEM261	physical	15231747
KGUA_HUMAN	GUK1	physical	15231747
PDIA1_HUMAN	P4HB	physical	15231747
FLNA_HUMAN	FLNA	physical	15231747
ARF4_HUMAN	ARF4	physical	15231747
4F2_HUMAN	SLC3A2	physical	15231747
MP2K1_HUMAN	MAP2K1	physical	15231747
HIRA_HUMAN	HIRA	physical	15231747
CD81_HUMAN	CD81	physical	15231747
IDD_HUMAN	DGCR2	physical	15231747
CAN1_HUMAN	CAPN1	physical	15231747
HBAZ_HUMAN	HBZ	physical	15231747
PDLI7_HUMAN	PDLIM7	physical	15231747
SEPT9_HUMAN	SEPT9	physical	15231747
MIC60_HUMAN	IMMT	physical	15231747
P5CR1_HUMAN	PYCR1	physical	15231747
BRCA1_HUMAN	BRCA1	physical	15231747
S27A5_HUMAN	SLC27A5	physical	15231747
NTM1A_HUMAN	NTMT1	physical	15231747
DHX30_HUMAN	DHX30	physical	15231747
CUTA_HUMAN	CUTA	physical	15231747
GTSE1_HUMAN	GTSE1	physical	15231747
FXL15_HUMAN	FBXL15	physical	15231747
COIA1_HUMAN	COL18A1	physical	15231747
IMP2L_HUMAN	IMMP2L	physical	15231747
COG7_HUMAN	COG7	physical	15231747
PPOX_HUMAN	PPOX	physical	15231747
CATB_HUMAN	CTSB	physical	15231747
PEX10_HUMAN	PEX10	physical	15231747
QCR1_HUMAN	UQCRC1	physical	15231747
PRDX3_HUMAN	PRDX3	physical	15231747
SDF2_HUMAN	SDF2	physical	15231747
B3GA3_HUMAN	B3GAT3	physical	15231747
EIF3K_HUMAN	EIF3K	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
WNK1_HUMAN	WNK1	physical	22863883
STAU1_HUMAN	STAU1	physical	23125841
NUCL_HUMAN	NCL	physical	16571724
KAT2B_HUMAN	KAT2B	physical	15834135
ING4_HUMAN	ING4	physical	23603392
MYC_HUMAN	MYC	physical	23603392
CUL2_HUMAN	CUL2	physical	22086907
VEGFA_HUMAN	VEGFA	physical	23109422
PGH2_HUMAN	PTGS2	physical	23109422
CHK1_HUMAN	CHEK1	physical	26344197
DNJC7_HUMAN	DNAJC7	physical	26344197
ROA3_HUMAN	HNRNPA3	physical	26344197
ROAA_HUMAN	HNRNPAB	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
PGK1_HUMAN	PGK1	physical	26344197
BLMH_HUMAN	BLMH	physical	26496610
MCAT_HUMAN	SLC25A20	physical	26496610
CETN2_HUMAN	CETN2	physical	26496610
DKC1_HUMAN	DKC1	physical	26496610
DYN2_HUMAN	DNM2	physical	26496610
IF4G1_HUMAN	EIF4G1	physical	26496610
ETFA_HUMAN	ETFA	physical	26496610
FACD2_HUMAN	FANCD2	physical	26496610
ACSL4_HUMAN	ACSL4	physical	26496610
MTOR_HUMAN	MTOR	physical	26496610
GOGA4_HUMAN	GOLGA4	physical	26496610
HEXA_HUMAN	HEXA	physical	26496610
ROA2_HUMAN	HNRNPA2B1	physical	26496610
ROAA_HUMAN	HNRNPAB	physical	26496610
HNRPC_HUMAN	HNRNPC	physical	26496610
HNRPK_HUMAN	HNRNPK	physical	26496610
HNRPU_HUMAN	HNRNPU	physical	26496610
DHB4_HUMAN	HSD17B4	physical	26496610
HSP76_HUMAN	HSPA6	physical	26496610
ITB4_HUMAN	ITGB4	physical	26496610
IF6_HUMAN	EIF6	physical	26496610
M3K4_HUMAN	MAP3K4	physical	26496610
MYH1_HUMAN	MYH1	physical	26496610
NHS_HUMAN	NHS	physical	26496610
YBOX1_HUMAN	YBX1	physical	26496610
PHLP_HUMAN	PDCL	physical	26496610
PLXB1_HUMAN	PLXNB1	physical	26496610
PPM1A_HUMAN	PPM1A	physical	26496610
RBM4_HUMAN	RBM4	physical	26496610
RET_HUMAN	RET	physical	26496610
SRSF6_HUMAN	SRSF6	physical	26496610
UAP1_HUMAN	UAP1	physical	26496610
TARB1_HUMAN	TARBP1	physical	26496610
GCFC2_HUMAN	GCFC2	physical	26496610
TLN1_HUMAN	TLN1	physical	26496610
TNR1A_HUMAN	TNFRSF1A	physical	26496610
BAG6_HUMAN	BAG6	physical	26496610
UBP11_HUMAN	USP11	physical	26496610
DYSF_HUMAN	DYSF	physical	26496610
NRP1_HUMAN	NRP1	physical	26496610
TAXB1_HUMAN	TAX1BP1	physical	26496610
FUBP3_HUMAN	FUBP3	physical	26496610
GT2D1_HUMAN	GTF2IRD1	physical	26496610
ESPL1_HUMAN	ESPL1	physical	26496610
RHG32_HUMAN	ARHGAP32	physical	26496610
C2CD5_HUMAN	C2CD5	physical	26496610
OSBL2_HUMAN	OSBPL2	physical	26496610
RBM8A_HUMAN	RBM8A	physical	26496610
ANM3_HUMAN	PRMT3	physical	26496610
SAP18_HUMAN	SAP18	physical	26496610
ABCA7_HUMAN	ABCA7	physical	26496610
TBB3_HUMAN	TUBB3	physical	26496610
PPIH_HUMAN	PPIH	physical	26496610
HNRPQ_HUMAN	SYNCRIP	physical	26496610
SRS10_HUMAN	SRSF10	physical	26496610
COG2_HUMAN	COG2	physical	26496610
FND3A_HUMAN	FNDC3A	physical	26496610
MORC2_HUMAN	MORC2	physical	26496610
DHX30_HUMAN	DHX30	physical	26496610
F120A_HUMAN	FAM120A	physical	26496610
UBP24_HUMAN	USP24	physical	26496610
ECM29_HUMAN	KIAA0368	physical	26496610
DICER_HUMAN	DICER1	physical	26496610
SIR5_HUMAN	SIRT5	physical	26496610
KLDC2_HUMAN	KLHDC2	physical	26496610
INT7_HUMAN	INTS7	physical	26496610
PKN3_HUMAN	PKN3	physical	26496610
PLPL8_HUMAN	PNPLA8	physical	26496610
CHMP5_HUMAN	CHMP5	physical	26496610
URFB1_HUMAN	UHRF1BP1	physical	26496610
RAIN_HUMAN	RASIP1	physical	26496610
PINX1_HUMAN	PINX1	physical	26496610
HEAT3_HUMAN	HEATR3	physical	26496610
P4R3B_HUMAN	SMEK2	physical	26496610
Z286A_HUMAN	ZNF286A	physical	26496610
GPBP1_HUMAN	GPBP1	physical	26496610
PDRG1_HUMAN	PDRG1	physical	26496610
MTMRD_HUMAN	SBF2	physical	26496610
TLN2_HUMAN	TLN2	physical	26496610
KLF16_HUMAN	KLF16	physical	26496610
OBSCN_HUMAN	OBSCN	physical	26496610
WDR24_HUMAN	WDR24	physical	26496610
GRIN1_HUMAN	GPRIN1	physical	26496610
RM55_HUMAN	MRPL55	physical	26496610
PTGR2_HUMAN	PTGR2	physical	26496610
PPR18_HUMAN	PPP1R18	physical	26496610
DDX51_HUMAN	DDX51	physical	26496610
HNRC1_HUMAN	HNRNPCL1	physical	26496610
FBW1A_HUMAN	BTRC	physical	23530064
HSPB1_HUMAN	HSPB1	physical	23530064

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 HNRPD_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165; LYS-251; LYS-341 ANDLYS-353, AND MASS SPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-345, AND MASS SPECTROMETRY.	15782174 [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-82; SER-190 AND THR-193,AND MASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-83, AND MASSSPECTROMETRY.	19369195 [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-190 AND THR-193, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.	18318008 [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-82; SER-83; SER-190 ANDTHR-193, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND THR-193, AND MASSSPECTROMETRY.	18691976 [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-80, AND MASSSPECTROMETRY.	19367720 [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 SER-80; SER-82; SER-83;SER-87 AND THR-91, AND MASS SPECTROMETRY.	17287340 [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 SER-190, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY.	16094384 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190 AND THR-193, ANDMASS SPECTROMETRY.	15302935 [Abstract]

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