dbPTM

HNRH2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HNRH2_MOUSE
UniProt AC	P70333
Protein Name	Heterogeneous nuclear ribonucleoprotein H2
Gene Name	Hnrnph2
Organism	Mus musculus (Mouse).
Sequence Length	449
Subcellular Localization	Nucleus, nucleoplasm.
Protein Description	This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG) (By similarity)..
Protein Sequence	MMLSTEGREGFVVKVRGLPWSCSAEEVMRFFSDCKIQNGTSGVRFIYTREGRPSGEAFVELESEDEVKLALKKDRETMGHRYVEVFKSNSVEMDWVLKHTGPNSPDTANDGFVRLRGLPFGCSKEEIVQFFSGLEIVPNGMTLPVDFQGRSTGEAFVQFASQEIAEKALKKHKERIGHRYIEIFKSSRAEVRTHYDPPRKLMTMQRPGPYDRPGAGRGYNSIGRGAGFERMRRGAYGGGYGGYDDYGGYNDGYGFGSDRFGRDLNYCFSGMSDHRYGDGGSSFQSTTGHCVHMRGLPYRATENDIYNFFSPLNPMRVHIEIGPDGRVTGEADVEFATHEDAVAAMAKDKANMQHRYVELFLNSTAGTSGGAYDHSYVELFLNSTAGASGGAYGSQMMGGMGLSNQSSYGGPASQQLSGGYGGGYGGQSSMSGYDQVLQENSSDYQSNLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MMLSTEGR -------CCCCCCCC	5.71	-
2	Acetylation	------MMLSTEGRE ------CCCCCCCCC	3.99	-
4	Phosphorylation	----MMLSTEGREGF ----CCCCCCCCCEE	13.40	24719451
21	Phosphorylation	KVRGLPWSCSAEEVM EEECCCCCCCHHHHH	9.03	24719451
23	Phosphorylation	RGLPWSCSAEEVMRF ECCCCCCCHHHHHHH	32.95	22942356
35	Ubiquitination	MRFFSDCKIQNGTSG HHHHHCCEEECCCCC	52.93	-
54	Phosphorylation	YTREGRPSGEAFVEL EEECCCCCCCEEEEE	48.15	28833060
63	Phosphorylation	EAFVELESEDEVKLA CEEEEECCHHHHEEE	64.07	25521595
77	Phosphorylation	ALKKDRETMGHRYVE EEHHHHHHHCCEEEE	29.37	-
88	Phosphorylation	RYVEVFKSNSVEMDW EEEEEHHCCCEEEEE	23.91	26643407
90	Phosphorylation	VEVFKSNSVEMDWVL EEEHHCCCEEEEEEE	26.92	26643407
100	Phosphorylation	MDWVLKHTGPNSPDT EEEEEECCCCCCCCC	53.39	24925903
104	Phosphorylation	LKHTGPNSPDTANDG EECCCCCCCCCCCCC	27.56	24925903
107	Phosphorylation	TGPNSPDTANDGFVR CCCCCCCCCCCCCEE	30.64	24925903
161	Phosphorylation	EAFVQFASQEIAEKA HHHHHHHHHHHHHHH	29.63	23684622
167	Acetylation	ASQEIAEKALKKHKE HHHHHHHHHHHHHHH	50.42	68907
167	Ubiquitination	ASQEIAEKALKKHKE HHHHHHHHHHHHHHH	50.42	-
180	Phosphorylation	KERIGHRYIEIFKSS HHHHCHHHHHHHHHC	9.38	24719451
186	Phosphorylation	RYIEIFKSSRAEVRT HHHHHHHHCCCCHHH	17.82	24719451
187	Phosphorylation	YIEIFKSSRAEVRTH HHHHHHHCCCCHHHC	35.78	24719451
206	Dimethylation	RKLMTMQRPGPYDRP CCCCCCCCCCCCCCC	27.59	-
206	Methylation	RKLMTMQRPGPYDRP CCCCCCCCCCCCCCC	27.59	18961487
212	Methylation	QRPGPYDRPGAGRGY CCCCCCCCCCCCCCC	26.21	18961497
212	Dimethylation	QRPGPYDRPGAGRGY CCCCCCCCCCCCCCC	26.21	-
217	Dimethylation	YDRPGAGRGYNSIGR CCCCCCCCCCCCCCC	43.84	-
217	Methylation	YDRPGAGRGYNSIGR CCCCCCCCCCCCCCC	43.84	25057133
224	Dimethylation	RGYNSIGRGAGFERM CCCCCCCCCCCHHHH	30.07	-
224	Methylation	RGYNSIGRGAGFERM CCCCCCCCCCCHHHH	30.07	25057137
230	Methylation	GRGAGFERMRRGAYG CCCCCHHHHHCCCCC	22.96	18960595
230	Dimethylation	GRGAGFERMRRGAYG CCCCCHHHHHCCCCC	22.96	-
233	Methylation	AGFERMRRGAYGGGY CCHHHHHCCCCCCCC	25.42	24129315
243	Phosphorylation	YGGGYGGYDDYGGYN CCCCCCCCCCCCCCC	10.98	22817900
246	Phosphorylation	GYGGYDDYGGYNDGY CCCCCCCCCCCCCCC	15.00	22817900
266	Phosphorylation	RFGRDLNYCFSGMSD CCCCCCCCCCCCCCC	11.36	25159016
269	Phosphorylation	RDLNYCFSGMSDHRY CCCCCCCCCCCCCCC	29.99	24719451
272	Phosphorylation	NYCFSGMSDHRYGDG CCCCCCCCCCCCCCC	33.52	25159016
290	S-nitrosocysteine	FQSTTGHCVHMRGLP CCCCCCCCEEECCCC	2.08	-
290	S-nitrosylation	FQSTTGHCVHMRGLP CCCCCCCCEEECCCC	2.08	20925432
306	Phosphorylation	RATENDIYNFFSPLN CCCCCCCHHCCCCCC	14.58	18563927
310	Phosphorylation	NDIYNFFSPLNPMRV CCCHHCCCCCCCCEE	25.08	22942356
384	Phosphorylation	VELFLNSTAGASGGA EEEHHCCCCCCCCCH	28.21	22802335
388	Phosphorylation	LNSTAGASGGAYGSQ HCCCCCCCCCHHHCC	36.52	22802335
392	Phosphorylation	AGASGGAYGSQMMGG CCCCCCHHHCCCCCC	22.15	22802335
394	Phosphorylation	ASGGAYGSQMMGGMG CCCCHHHCCCCCCCC	11.39	22802335
403	Phosphorylation	MMGGMGLSNQSSYGG CCCCCCCCCCCCCCC	27.39	22802335
406	Phosphorylation	GMGLSNQSSYGGPAS CCCCCCCCCCCCCHH	29.76	22802335
407	Phosphorylation	MGLSNQSSYGGPASQ CCCCCCCCCCCCHHH	20.31	22802335
408	Phosphorylation	GLSNQSSYGGPASQQ CCCCCCCCCCCHHHC	31.20	22802335

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
104	S	Phosphorylation	Kinase	MAPK1	P63085	GPS
104	S	Phosphorylation	Kinase	MAPK14	P47811	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HNRH2_MOUSE !!

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 HNRH2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HNRH2_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HNRH2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND THR-107, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.	14729942 [Abstract]