dbPTM

HNRH3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HNRH3_HUMAN
UniProt AC	P31942
Protein Name	Heterogeneous nuclear ribonucleoprotein H3
Gene Name	HNRNPH3
Organism	Homo sapiens (Human).
Sequence Length	346
Subcellular Localization	Nucleus .
Protein Description	Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction..
Protein Sequence	MDWVMKHNGPNDASDGTVRLRGLPFGCSKEEIVQFFQGLEIVPNGITLTMDYQGRSTGEAFVQFASKEIAENALGKHKERIGHRYIEIFRSSRSEIKGFYDPPRRLLGQRPGPYDRPIGGRGGYYGAGRGSMYDRMRRGGDGYDGGYGGFDDYGGYNNYGYGNDGFDDRMRDGRGMGGHGYGGAGDASSGFHGGHFVHMRGLPFRATENDIANFFSPLNPIRVHIDIGADGRATGEADVEFVTHEDAVAAMSKDKNNMQHRYIELFLNSTPGGGSGMGGSGMGGYGRDGMDNQGGYGSVGRMGMGNNYSGGYGTPDGLGGYGRGGGGSGGYYGQGGMSGGGWRGMY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDWVMKHN -------CCCCCCCC	9.15	-
4 (in isoform 6)	Phosphorylation	-	2.97	24043423
6	Sumoylation	--MDWVMKHNGPNDA --CCCCCCCCCCCCC	25.05	-
6	Acetylation	--MDWVMKHNGPNDA --CCCCCCCCCCCCC	25.05	25825284
6	Methylation	--MDWVMKHNGPNDA --CCCCCCCCCCCCC	25.05	109061911
6	Sumoylation	--MDWVMKHNGPNDA --CCCCCCCCCCCCC	25.05	28112733
6	Ubiquitination	--MDWVMKHNGPNDA --CCCCCCCCCCCCC	25.05	21890473
7 (in isoform 6)	Phosphorylation	-	26.78	24043423
8 (in isoform 6)	Phosphorylation	-	63.20	24043423
10 (in isoform 6)	Phosphorylation	-	40.62	24043423
16 (in isoform 6)	Phosphorylation	-	24.50	24043423
17	Phosphorylation	PNDASDGTVRLRGLP CCCCCCCCEEECCCC	13.88	-
18 (in isoform 3)	Ubiquitination	-	7.11	21890473
19	Methylation	DASDGTVRLRGLPFG CCCCCCEEECCCCCC	20.64	115478855
19 (in isoform 6)	Phosphorylation	-	20.64	24043423
22 (in isoform 6)	Phosphorylation	-	42.15	24043423
24 (in isoform 6)	Phosphorylation	-	26.80	24043423
27 (in isoform 3)	Ubiquitination	-	5.56	21890473
28	Phosphorylation	RGLPFGCSKEEIVQF CCCCCCCCHHHHHHH	43.40	22777824
47	Phosphorylation	EIVPNGITLTMDYQG EECCCCEEEEEEECC	19.99	-
48 (in isoform 3)	Ubiquitination	-	3.36	21890473
49	Phosphorylation	VPNGITLTMDYQGRS CCCCEEEEEEECCCC	10.19	-
52	Phosphorylation	GITLTMDYQGRSTGE CEEEEEEECCCCHHH	11.31	-
57	Phosphorylation	MDYQGRSTGEAFVQF EEECCCCHHHHHHHH	37.37	21712546
66	Phosphorylation	EAFVQFASKEIAENA HHHHHHHCHHHHHHH	31.91	21712546
67	Acetylation	AFVQFASKEIAENAL HHHHHHCHHHHHHHH	50.11	26051181
67	Sumoylation	AFVQFASKEIAENAL HHHHHHCHHHHHHHH	50.11	28112733
67	Ubiquitination	AFVQFASKEIAENAL HHHHHHCHHHHHHHH	50.11	21906983
67 (in isoform 1)	Ubiquitination	-	50.11	21890473
67 (in isoform 2)	Ubiquitination	-	50.11	21890473
76	Acetylation	IAENALGKHKERIGH HHHHHHHHHHHHHCH	52.97	25953088
76	Ubiquitination	IAENALGKHKERIGH HHHHHHHHHHHHHCH	52.97	21906983
76 (in isoform 1)	Ubiquitination	-	52.97	21890473
76 (in isoform 2)	Ubiquitination	-	52.97	21890473
78	Ubiquitination	ENALGKHKERIGHRY HHHHHHHHHHHCHHH	52.77	-
90	Methylation	HRYIEIFRSSRSEIK HHHHHHHHCCHHHHC	39.11	115478863
91	Phosphorylation	RYIEIFRSSRSEIKG HHHHHHHCCHHHHCC	21.25	28348404
92	Phosphorylation	YIEIFRSSRSEIKGF HHHHHHCCHHHHCCC	35.25	28348404
97	Ubiquitination	RSSRSEIKGFYDPPR HCCHHHHCCCCCCHH	38.63	21890473
97 (in isoform 1)	Ubiquitination	-	38.63	21890473
97 (in isoform 2)	Ubiquitination	-	38.63	21890473
100	Phosphorylation	RSEIKGFYDPPRRLL HHHHCCCCCCHHHHC	35.89	28796482
110	Methylation	PRRLLGQRPGPYDRP HHHHCCCCCCCCCCC	36.02	81121133
116	Methylation	QRPGPYDRPIGGRGG CCCCCCCCCCCCCCC	20.92	24395495
116 (in isoform 2)	Methylation	-	20.92	24129315
121	Asymmetric dimethylarginine	YDRPIGGRGGYYGAG CCCCCCCCCCCCCCC	30.10	-
121	Methylation	YDRPIGGRGGYYGAG CCCCCCCCCCCCCCC	30.10	11152131
121 (in isoform 2)	Methylation	-	30.10	24129315
125	Phosphorylation	IGGRGGYYGAGRGSM CCCCCCCCCCCCCHH	12.08	25884760
129	Dimethylation	GGYYGAGRGSMYDRM CCCCCCCCCHHHHHH	33.22	-
129	Methylation	GGYYGAGRGSMYDRM CCCCCCCCCHHHHHH	33.22	24383093
129 (in isoform 2)	Methylation	-	33.22	24129315
131 (in isoform 2)	Phosphorylation	-	16.89	26846344
132 (in isoform 2)	Phosphorylation	-	4.49	26846344
133	Phosphorylation	GAGRGSMYDRMRRGG CCCCCHHHHHHHCCC	11.33	25884760
135	Dimethylation	GRGSMYDRMRRGGDG CCCHHHHHHHCCCCC	11.74	-
135	Methylation	GRGSMYDRMRRGGDG CCCHHHHHHHCCCCC	11.74	30762319
138	Methylation	SMYDRMRRGGDGYDG HHHHHHHCCCCCCCC	44.07	59080961
138 (in isoform 2)	Phosphorylation	-	44.07	26846344
141 (in isoform 2)	Phosphorylation	-	56.13	26846344
143	Phosphorylation	MRRGGDGYDGGYGGF HHCCCCCCCCCCCCC	19.02	22817900
144 (in isoform 2)	Phosphorylation	-	49.96	26846344
146 (in isoform 2)	Phosphorylation	-	18.27	26846344
147	Phosphorylation	GDGYDGGYGGFDDYG CCCCCCCCCCCCCCC	21.43	20090780
153	Phosphorylation	GYGGFDDYGGYNNYG CCCCCCCCCCCCCCC	17.81	22817900
156	Phosphorylation	GFDDYGGYNNYGYGN CCCCCCCCCCCCCCC	8.89	20090780
159	Phosphorylation	DYGGYNNYGYGNDGF CCCCCCCCCCCCCCC	14.21	22817900
161	Phosphorylation	GGYNNYGYGNDGFDD CCCCCCCCCCCCCCC	11.46	24043423
174	Methylation	DDRMRDGRGMGGHGY CCCCCCCCCCCCCCC	35.89	24129315
181	Phosphorylation	RGMGGHGYGGAGDAS CCCCCCCCCCCCCCC	13.50	20090780
188	Phosphorylation	YGGAGDASSGFHGGH CCCCCCCCCCCCCCE	35.42	29449344
189	O-linked_Glycosylation	GGAGDASSGFHGGHF CCCCCCCCCCCCCEE	47.39	28510447
189	Phosphorylation	GGAGDASSGFHGGHF CCCCCCCCCCCCCEE	47.39	27251275
200	Methylation	GGHFVHMRGLPFRAT CCEEEEECCCCCCCC	28.72	115478847
207	Phosphorylation	RGLPFRATENDIANF CCCCCCCCCCHHHHH	30.94	23403867
216	Phosphorylation	NDIANFFSPLNPIRV CHHHHHCCCCCCEEE	25.08	29255136
262	Phosphorylation	KNNMQHRYIELFLNS CCCCCCEEEEEHHCC	9.16	23663014
269	Phosphorylation	YIELFLNSTPGGGSG EEEEHHCCCCCCCCC	37.82	25159151
270	Phosphorylation	IELFLNSTPGGGSGM EEEHHCCCCCCCCCC	25.53	25159151
275	Phosphorylation	NSTPGGGSGMGGSGM CCCCCCCCCCCCCCC	28.96	23663014
280	Phosphorylation	GGSGMGGSGMGGYGR CCCCCCCCCCCCCCC	21.63	23663014
285	Phosphorylation	GGSGMGGYGRDGMDN CCCCCCCCCCCCCCC	11.85	23663014
287	Methylation	SGMGGYGRDGMDNQG CCCCCCCCCCCCCCC	28.91	-
290	Sulfoxidation	GGYGRDGMDNQGGYG CCCCCCCCCCCCCCC	5.25	21406390
296	Phosphorylation	GMDNQGGYGSVGRMG CCCCCCCCCCCCCCC	17.04	27273156
298	Phosphorylation	DNQGGYGSVGRMGMG CCCCCCCCCCCCCCC	16.96	25159151
301	Methylation	GGYGSVGRMGMGNNY CCCCCCCCCCCCCCC	19.14	18600907
308	Phosphorylation	RMGMGNNYSGGYGTP CCCCCCCCCCCCCCC	16.82	18180459
309	Phosphorylation	MGMGNNYSGGYGTPD CCCCCCCCCCCCCCC	28.06	30576142
312	Phosphorylation	GNNYSGGYGTPDGLG CCCCCCCCCCCCCCC	22.73	18180459
314	Phosphorylation	NYSGGYGTPDGLGGY CCCCCCCCCCCCCCC	15.10	25159151
321	Phosphorylation	TPDGLGGYGRGGGGS CCCCCCCCCCCCCCC	11.23	20090780
323	Dimethylation	DGLGGYGRGGGGSGG CCCCCCCCCCCCCCC	31.90	-
323	Methylation	DGLGGYGRGGGGSGG CCCCCCCCCCCCCCC	31.90	24129315
328	Phosphorylation	YGRGGGGSGGYYGQG CCCCCCCCCCCCCCC	32.11	21945579
331	Phosphorylation	GGGGSGGYYGQGGMS CCCCCCCCCCCCCCC	14.14	21945579
332	Phosphorylation	GGGSGGYYGQGGMSG CCCCCCCCCCCCCCC	13.27	21945579
338	Phosphorylation	YYGQGGMSGGGWRGM CCCCCCCCCCCCCCC	37.25	21945579
343	Dimethylation	GMSGGGWRGMY---- CCCCCCCCCCC----	24.23	-
343	Methylation	GMSGGGWRGMY---- CCCCCCCCCCC----	24.23	24129315
346	Phosphorylation	GGGWRGMY------- CCCCCCCC-------	20.44	22210691

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 HNRH3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HNRH3_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 HNRH3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANX11_HUMAN	ANXA11	physical	16169070
PIM2_HUMAN	PIM2	physical	16169070
RS4X_HUMAN	RPS4X	physical	16169070
TTHY_HUMAN	TTR	physical	16169070
ERG28_HUMAN	C14orf1	physical	16169070
KAT5_HUMAN	KAT5	physical	16169070
UT14A_HUMAN	UTP14A	physical	16169070
DPYL1_HUMAN	CRMP1	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
ROA2_HUMAN	HNRNPA2B1	physical	22939629
ROA1_HUMAN	HNRNPA1	physical	22939629
HNRPR_HUMAN	HNRNPR	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
HNRPF_HUMAN	HNRNPF	physical	22939629
SF3A3_HUMAN	SF3A3	physical	22939629
HNRL1_HUMAN	HNRNPUL1	physical	22939629
SNRPA_HUMAN	SNRPA	physical	22939629
SSBP_HUMAN	SSBP1	physical	22939629
PUF60_HUMAN	PUF60	physical	22939629
CHERP_HUMAN	CHERP	physical	22365833
ROA0_HUMAN	HNRNPA0	physical	22365833
ROA1_HUMAN	HNRNPA1	physical	22365833
NCBP3_HUMAN	C17orf85	physical	22365833
DDX17_HUMAN	DDX17	physical	22365833
DDX5_HUMAN	DDX5	physical	22365833
HNRPU_HUMAN	HNRNPU	physical	22365833
HNRL1_HUMAN	HNRNPUL1	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
HNRPD_HUMAN	HNRNPD	physical	22365833
HNRPF_HUMAN	HNRNPF	physical	22365833
HNRH1_HUMAN	HNRNPH1	physical	22365833
HNRH3_HUMAN	HNRNPH3	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
HNRDL_HUMAN	HNRNPDL	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197
SC16A_HUMAN	SEC16A	physical	26344197
STIP1_HUMAN	STIP1	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 HNRH3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-216, AND MASS SPECTROMETRY.	19413330 [Abstract]
Methylation
Reference	PubMed
"A post-translational modification of nuclear proteins, N(G),N(G)-dimethyl-Arg, found in a natural HLA class I peptide ligand."; Yague J., Vazquez J., Lopez de Castro J.A.; Protein Sci. 9:2210-2217(2000). Cited for: PROTEIN SEQUENCE OF 116-127, AND METHYLATION AT ARG-121.	11152131 [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-216; SER-298 ANDTHR-314, 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-216, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-216, AND MASS SPECTROMETRY.	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-216, AND MASSSPECTROMETRY.	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-216, AND MASSSPECTROMETRY.	18691976 [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-216, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-296, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-296, AND MASSSPECTROMETRY.	15592455 [Abstract]