dbPTM

HNRPF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HNRPF_HUMAN
UniProt AC	P52597
Protein Name	Heterogeneous nuclear ribonucleoprotein F
Gene Name	HNRNPF
Organism	Homo sapiens (Human).
Sequence Length	415
Subcellular Localization	Nucleus, nucleoplasm.
Protein Description	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. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state..
Protein Sequence	MMLGPEGGEGFVVKLRGLPWSCSVEDVQNFLSDCTIHDGAAGVHFIYTREGRQSGEAFVELGSEDDVKMALKKDRESMGHRYIEVFKSHRTEMDWVLKHSGPNSADSANDGFVRLRGLPFGCTKEEIVQFFSGLEIVPNGITLPVDPEGKITGEAFVQFASQELAEKALGKHKERIGHRYIEVFKSSQEEVRSYSDPPLKFMSVQRPGPYDRPGTARRYIGIVKQAGLERMRPGAYSTGYGGYEEYSGLSDGYGFTTDLFGRDLSYCLSGMYDHRYGDSEFTVQSTTGHCVHMRGLPYKATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEEAVAAMSKDRANMQHRYIELFLNSTTGASNGAYSSQVMQGMGVSAAQATYSGLESQSVSGCYGAGYSGQNSMGGYD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MMLGPEGG -------CCCCCCCC	4.52	22814378
2	Acetylation	------MMLGPEGGE ------CCCCCCCCC	6.27	22223895
2	Sulfoxidation	------MMLGPEGGE ------CCCCCCCCC	6.27	28183972
14	Ubiquitination	GGEGFVVKLRGLPWS CCCCEEEEECCCCCC	27.45	21906983
21	Phosphorylation	KLRGLPWSCSVEDVQ EECCCCCCCCHHHHH	8.45	28464451
23	Phosphorylation	RGLPWSCSVEDVQNF CCCCCCCCHHHHHHH	24.03	28464451
32	Phosphorylation	EDVQNFLSDCTIHDG HHHHHHHHCCEEECC	26.88	28464451
35	Phosphorylation	QNFLSDCTIHDGAAG HHHHHCCEEECCCCE	26.74	28464451
54	Phosphorylation	YTREGRQSGEAFVEL EECCCCCCCCEEEEE	36.92	29214152
63	Phosphorylation	EAFVELGSEDDVKMA CEEEEECCHHHHHHH	50.94	20873877
68	Sumoylation	LGSEDDVKMALKKDR ECCHHHHHHHHHHHH	26.00	-
68	Ubiquitination	LGSEDDVKMALKKDR ECCHHHHHHHHHHHH	26.00	-
72	Sumoylation	DDVKMALKKDRESMG HHHHHHHHHHHHHHC	42.99	-
72	Sumoylation	DDVKMALKKDRESMG HHHHHHHHHHHHHHC	42.99	15161980
77	Phosphorylation	ALKKDRESMGHRYIE HHHHHHHHHCHHHHH	30.84	29496963
82	Phosphorylation	RESMGHRYIEVFKSH HHHHCHHHHHHHHHC	8.85	23663014
87	Methylation	HRYIEVFKSHRTEMD HHHHHHHHHCHHHCE	50.99	19608861
87	Acetylation	HRYIEVFKSHRTEMD HHHHHHHHHCHHHCE	50.99	25825284
87	Ubiquitination	HRYIEVFKSHRTEMD HHHHHHHHHCHHHCE	50.99	21890473
87	Malonylation	HRYIEVFKSHRTEMD HHHHHHHHHCHHHCE	50.99	26320211
87	Sumoylation	HRYIEVFKSHRTEMD HHHHHHHHHCHHHCE	50.99	28112733
90	Methylation	IEVFKSHRTEMDWVL HHHHHHCHHHCEEHH	39.20	115479107
93	Sulfoxidation	FKSHRTEMDWVLKHS HHHCHHHCEEHHHCC	4.93	28183972
98	Acetylation	TEMDWVLKHSGPNSA HHCEEHHHCCCCCCC	26.55	21466224
98	Ubiquitination	TEMDWVLKHSGPNSA HHCEEHHHCCCCCCC	26.55	21890473
98	Malonylation	TEMDWVLKHSGPNSA HHCEEHHHCCCCCCC	26.55	26320211
100	Phosphorylation	MDWVLKHSGPNSADS CEEHHHCCCCCCCCC	55.12	30266825
104	Phosphorylation	LKHSGPNSADSANDG HHCCCCCCCCCCCCC	36.26	29255136
107	Phosphorylation	SGPNSADSANDGFVR CCCCCCCCCCCCCEE	28.78	30266825
114	Methylation	SANDGFVRLRGLPFG CCCCCCEEECCCCCC	19.19	115479091
142	Phosphorylation	EIVPNGITLPVDPEG EECCCCEEEECCCCC	26.80	18452278
150	Sumoylation	LPVDPEGKITGEAFV EECCCCCCCCHHHHH	35.12	-
152	Phosphorylation	VDPEGKITGEAFVQF CCCCCCCCHHHHHHH	32.24	27251275
161	Phosphorylation	EAFVQFASQELAEKA HHHHHHHCHHHHHHH	26.02	17525332
167	Ubiquitination	ASQELAEKALGKHKE HCHHHHHHHHHHHHH	43.22	21906983
167	Sumoylation	ASQELAEKALGKHKE HCHHHHHHHHHHHHH	43.22	28112733
167	Acetylation	ASQELAEKALGKHKE HCHHHHHHHHHHHHH	43.22	26051181
171	Ubiquitination	LAEKALGKHKERIGH HHHHHHHHHHHHHCH	52.97	-
180	Phosphorylation	KERIGHRYIEVFKSS HHHHCHHHHHHHHCC	8.85	23403867
185	Sumoylation	HRYIEVFKSSQEEVR HHHHHHHHCCHHHHH	55.14	-
185	Ubiquitination	HRYIEVFKSSQEEVR HHHHHHHHCCHHHHH	55.14	21890473
185	Sumoylation	HRYIEVFKSSQEEVR HHHHHHHHCCHHHHH	55.14	28112733
185	Acetylation	HRYIEVFKSSQEEVR HHHHHHHHCCHHHHH	55.14	26051181
186	Phosphorylation	RYIEVFKSSQEEVRS HHHHHHHCCHHHHHH	26.28	30266825
187	Phosphorylation	YIEVFKSSQEEVRSY HHHHHHCCHHHHHHC	42.05	30266825
193	Phosphorylation	SSQEEVRSYSDPPLK CCHHHHHHCCCCCCE	33.88	28152594
194	Phosphorylation	SQEEVRSYSDPPLKF CHHHHHHCCCCCCEE	13.41	28152594
195	Phosphorylation	QEEVRSYSDPPLKFM HHHHHHCCCCCCEEE	44.91	21815630
200	Acetylation	SYSDPPLKFMSVQRP HCCCCCCEEEEECCC	44.81	27452117
200	Sumoylation	SYSDPPLKFMSVQRP HCCCCCCEEEEECCC	44.81	-
200	Ubiquitination	SYSDPPLKFMSVQRP HCCCCCCEEEEECCC	44.81	21906983
200	Sumoylation	SYSDPPLKFMSVQRP HCCCCCCEEEEECCC	44.81	28112733
202	Sulfoxidation	SDPPLKFMSVQRPGP CCCCCEEEEECCCCC	3.52	28183972
203	Phosphorylation	DPPLKFMSVQRPGPY CCCCEEEEECCCCCC	20.45	28796482
210	Phosphorylation	SVQRPGPYDRPGTAR EECCCCCCCCCCCHH	30.42	25101063
212	Dimethylation	QRPGPYDRPGTARRY CCCCCCCCCCCHHHH	26.21	-
212	Methylation	QRPGPYDRPGTARRY CCCCCCCCCCCHHHH	26.21	54556609
215	Phosphorylation	GPYDRPGTARRYIGI CCCCCCCCHHHHHHH	21.48	23401153
217	Methylation	YDRPGTARRYIGIVK CCCCCCHHHHHHHHH	31.60	54556617
218	Methylation	DRPGTARRYIGIVKQ CCCCCHHHHHHHHHH	25.59	80702355
219	Phosphorylation	RPGTARRYIGIVKQA CCCCHHHHHHHHHHH	9.65	28152594
224	Methylation	RRYIGIVKQAGLERM HHHHHHHHHHCHHHC	32.29	22641049
224	Acetylation	RRYIGIVKQAGLERM HHHHHHHHHHCHHHC	32.29	19608861
224	Sumoylation	RRYIGIVKQAGLERM HHHHHHHHHHCHHHC	32.29	-
224	Ubiquitination	RRYIGIVKQAGLERM HHHHHHHHHHCHHHC	32.29	21906983
224	Sumoylation	RRYIGIVKQAGLERM HHHHHHHHHHCHHHC	32.29	28112733
231	Sulfoxidation	KQAGLERMRPGAYST HHHCHHHCCCCCCCC	4.41	28183972
232	Methylation	QAGLERMRPGAYSTG HHCHHHCCCCCCCCC	32.49	115479099
236	Phosphorylation	ERMRPGAYSTGYGGY HHCCCCCCCCCCCCC	16.81	22817900
237	Phosphorylation	RMRPGAYSTGYGGYE HCCCCCCCCCCCCCC	18.15	28348404
238	Phosphorylation	MRPGAYSTGYGGYEE CCCCCCCCCCCCCCC	23.03	21082442
240	Phosphorylation	PGAYSTGYGGYEEYS CCCCCCCCCCCCCCC	13.89	22817900
243	Phosphorylation	YSTGYGGYEEYSGLS CCCCCCCCCCCCCCC	10.96	22817900
246	Phosphorylation	GYGGYEEYSGLSDGY CCCCCCCCCCCCCCC	8.97	27259358
247	Phosphorylation	YGGYEEYSGLSDGYG CCCCCCCCCCCCCCC	36.22	-
250	Phosphorylation	YEEYSGLSDGYGFTT CCCCCCCCCCCCCCH	32.30	24275569
253	Phosphorylation	YSGLSDGYGFTTDLF CCCCCCCCCCCHHHC	17.66	20090780
265	Phosphorylation	DLFGRDLSYCLSGMY HHCCCCHHHHHHCCC	20.35	25159151
265	O-linked_Glycosylation	DLFGRDLSYCLSGMY HHCCCCHHHHHHCCC	20.35	23301498
266	Phosphorylation	LFGRDLSYCLSGMYD HCCCCHHHHHHCCCC	12.52	27134283
267	Glutathionylation	FGRDLSYCLSGMYDH CCCCHHHHHHCCCCC	1.88	22555962
269	Phosphorylation	RDLSYCLSGMYDHRY CCHHHHHHCCCCCCC	20.25	30576142
272	Phosphorylation	SYCLSGMYDHRYGDS HHHHHCCCCCCCCCC	16.48	29978859
276	Phosphorylation	SGMYDHRYGDSEFTV HCCCCCCCCCCEEEE	23.12	23312004
279	Phosphorylation	YDHRYGDSEFTVQST CCCCCCCCEEEEEEC	30.19	28442448
282	Phosphorylation	RYGDSEFTVQSTTGH CCCCCEEEEEECCCC	17.37	28442448
285	Phosphorylation	DSEFTVQSTTGHCVH CCEEEEEECCCCEEE	24.49	23312004
286	Phosphorylation	SEFTVQSTTGHCVHM CEEEEEECCCCEEEE	21.50	23312004
287	Phosphorylation	EFTVQSTTGHCVHMR EEEEEECCCCEEEEC	30.12	23312004
290	Glutathionylation	VQSTTGHCVHMRGLP EEECCCCEEEECCCC	2.08	22555962
299	Ubiquitination	HMRGLPYKATENDIY EECCCCCCCCCCCCH	47.06	21906983
301	Phosphorylation	RGLPYKATENDIYNF CCCCCCCCCCCCHHC	31.04	27987026
306	Phosphorylation	KATENDIYNFFSPLN CCCCCCCHHCCCCCC	14.58	29255136
310	Phosphorylation	NDIYNFFSPLNPVRV CCCHHCCCCCCCEEE	25.08	29255136
328	Phosphorylation	IGPDGRVTGEADVEF ECCCCCCCEECCEEE	28.13	-
337	Phosphorylation	EADVEFATHEEAVAA ECCEEEHHHHHHHHH	34.83	21601212
346	Phosphorylation	EEAVAAMSKDRANMQ HHHHHHHCHHCHHHH	27.03	21601212
347	Ubiquitination	EAVAAMSKDRANMQH HHHHHHCHHCHHHHH	37.84	-
401	Phosphorylation	SQSVSGCYGAGYSGQ CCCCCCCCCCCCCCC	17.34	22817900
406	Phosphorylation	GCYGAGYSGQNSMGG CCCCCCCCCCCCCCC	32.74	26074081
410	Phosphorylation	AGYSGQNSMGGYD-- CCCCCCCCCCCCC--	15.77	26074081
414	Phosphorylation	GQNSMGGYD------ CCCCCCCCC------	16.86	26074081

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 HNRPF_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RBMX_HUMAN	RBMX	physical	22939629
HNRPK_HUMAN	HNRNPK	physical	22939629
HNRPR_HUMAN	HNRNPR	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
HNRPM_HUMAN	HNRNPM	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
RBP2_HUMAN	RANBP2	physical	22939629
MIRO2_HUMAN	RHOT2	physical	22939629
MOGS_HUMAN	MOGS	physical	22939629
NOL11_HUMAN	NOL11	physical	22939629
PLP2_HUMAN	PLP2	physical	22939629
PEX3_HUMAN	PEX3	physical	22939629
RAB21_HUMAN	RAB21	physical	22939629
NDUF4_HUMAN	NDUFAF4	physical	22939629
RAB14_HUMAN	RAB14	physical	22939629
RADI_HUMAN	RDX	physical	22939629
RU1C_HUMAN	SNRPC	physical	22365833
SF3B4_HUMAN	SF3B4	physical	22365833
SF01_HUMAN	SF1	physical	22365833
ROA0_HUMAN	HNRNPA0	physical	22365833
HNRL1_HUMAN	HNRNPUL1	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
HNRPD_HUMAN	HNRNPD	physical	22365833
HNRH3_HUMAN	HNRNPH3	physical	22365833
TOE1_HUMAN	TOE1	physical	22365833
RFOX2_HUMAN	RBFOX2	physical	22365833
TGM2_HUMAN	TGM2	physical	21988832
ARP3_HUMAN	ACTR3	physical	22863883
ZPR1_HUMAN	ZPR1	physical	22863883
HNRPM_HUMAN	HNRNPM	physical	25416956
DZIP3_HUMAN	DZIP3	physical	25416956
TFG_HUMAN	TFG	physical	25416956
HNRL1_HUMAN	HNRNPUL1	physical	25416956
IKZF3_HUMAN	IKZF3	physical	25416956
RFOX2_HUMAN	RBFOX2	physical	25416956
4ET_HUMAN	EIF4ENIF1	physical	25416956
CCD33_HUMAN	CCDC33	physical	25416956
CA094_HUMAN	C1orf94	physical	25416956
HSFY1_HUMAN	HSFY1	physical	25416956
BASP1_HUMAN	BASP1	physical	26344197
PUF60_HUMAN	PUF60	physical	26344197
CCD33_HUMAN	CCDC33	physical	21516116
CARF_HUMAN	CDKN2AIP	physical	28514442
ZCHC8_HUMAN	ZCCHC8	physical	28514442
ACOX1_HUMAN	ACOX1	physical	28514442
SPT5H_HUMAN	SUPT5H	physical	28514442
DPP9_HUMAN	DPP9	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.

Regulatory Network of HNRPF_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 AND MET-2, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-87 AND LYS-224, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-104 AND SER-310, ANDMASS SPECTROMETRY.	19369195 [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-187 AND SER-310, ANDMASS SPECTROMETRY.	18691976 [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-310, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASSSPECTROMETRY.	17525332 [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-310, AND MASSSPECTROMETRY.	17081983 [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-310, AND MASSSPECTROMETRY.	15302935 [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-246, AND MASSSPECTROMETRY.	15592455 [Abstract]
Sumoylation
Reference	PubMed
"Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc fingerproteins, and nuclear pore complex proteins: a proteomic analysis."; Li T., Evdokimov E., Shen R.F., Chao C.C., Tekle E., Wang T.,Stadtman E.R., Yang D.C., Chock P.B.; Proc. Natl. Acad. Sci. U.S.A. 101:8551-8556(2004). Cited for: SUMOYLATION AT LYS-72.	15161980 [Abstract]