dbPTM

PRP4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRP4_HUMAN
UniProt AC	O43172
Protein Name	U4/U6 small nuclear ribonucleoprotein Prp4
Gene Name	PRPF4
Organism	Homo sapiens (Human).
Sequence Length	522
Subcellular Localization	Nucleus speckle . Colocalizes with spliceosomal snRNPs..
Protein Description	Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome..
Protein Sequence	MASSRASSTQATKTKAPDDLVAPVVKKPHIYYGSLEEKERERLAKGESGILGKDGLKAGIEAGNINITSGEVFEIEEHISERQAEVLAEFERRKRARQINVSTDDSEVKACLRALGEPITLFGEGPAERRERLRNILSVVGTDALKKTKKDDEKSKKSKEEYQQTWYHEGPNSLKVARLWIANYSLPRAMKRLEEARLHKEIPETTRTSQMQELHKSLRSLNNFCSQIGDDRPISYCHFSPNSKMLATACWSGLCKLWSVPDCNLLHTLRGHNTNVGAIVFHPKSTVSLDPKDVNLASCAADGSVKLWSLDSDEPVADIEGHTVRVARVMWHPSGRFLGTTCYDRSWRLWDLEAQEEILHQEGHSMGVYDIAFHQDGSLAGTGGLDAFGRVWDLRTGRCIMFLEGHLKEIYGINFSPNGYHIATGSGDNTCKVWDLRQRRCVYTIPAHQNLVTGVKFEPIHGNFLLTGAYDNTAKIWTHPGWSPLKTLAGHEGKVMGLDISSDGQLIATCSYDRTFKLWMAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MASSRASSTQATKT -CCCCCCCCCCCCCC	32.57	29083192
8	Phosphorylation	MASSRASSTQATKTK CCCCCCCCCCCCCCC	24.45	29083192
9	Phosphorylation	ASSRASSTQATKTKA CCCCCCCCCCCCCCC	21.52	29083192
12	Phosphorylation	RASSTQATKTKAPDD CCCCCCCCCCCCCCC	29.45	29083192
14	O-linked_Glycosylation	SSTQATKTKAPDDLV CCCCCCCCCCCCCCC	28.25	30379171
15	Sumoylation	STQATKTKAPDDLVA CCCCCCCCCCCCCCC	60.52	-
15	Sumoylation	STQATKTKAPDDLVA CCCCCCCCCCCCCCC	60.52	-
15	Acetylation	STQATKTKAPDDLVA CCCCCCCCCCCCCCC	60.52	26051181
27	Sumoylation	LVAPVVKKPHIYYGS CCCCCCCCCCEEECC	30.16	-
27	Malonylation	LVAPVVKKPHIYYGS CCCCCCCCCCEEECC	30.16	26320211
27	Sumoylation	LVAPVVKKPHIYYGS CCCCCCCCCCEEECC	30.16	19608861
27	Ubiquitination	LVAPVVKKPHIYYGS CCCCCCCCCCEEECC	30.16	19608861
27	Acetylation	LVAPVVKKPHIYYGS CCCCCCCCCCEEECC	30.16	19608861
31	Phosphorylation	VVKKPHIYYGSLEEK CCCCCCEEECCCCHH	9.95	28796482
32	Phosphorylation	VKKPHIYYGSLEEKE CCCCCEEECCCCHHH	10.31	28796482
34	Phosphorylation	KPHIYYGSLEEKERE CCCEEECCCCHHHHH	19.24	28796482
38	Acetylation	YYGSLEEKERERLAK EECCCCHHHHHHHHC	53.33	26051181
38	Ubiquitination	YYGSLEEKERERLAK EECCCCHHHHHHHHC	53.33	-
45	Sumoylation	KERERLAKGESGILG HHHHHHHCCCCCCCC	68.73	-
45	Ubiquitination	KERERLAKGESGILG HHHHHHHCCCCCCCC	68.73	-
45	2-Hydroxyisobutyrylation	KERERLAKGESGILG HHHHHHHCCCCCCCC	68.73	-
45	Sumoylation	KERERLAKGESGILG HHHHHHHCCCCCCCC	68.73	-
53	Acetylation	GESGILGKDGLKAGI CCCCCCCCHHHHCCE	45.22	23749302
53	2-Hydroxyisobutyrylation	GESGILGKDGLKAGI CCCCCCCCHHHHCCE	45.22	-
53	Ubiquitination	GESGILGKDGLKAGI CCCCCCCCHHHHCCE	45.22	-
109	Acetylation	STDDSEVKACLRALG CCCHHHHHHHHHHHC	29.36	26051181
146	Acetylation	VVGTDALKKTKKDDE HHCHHHHHHCCCCCH	61.18	25953088
146	2-Hydroxyisobutyrylation	VVGTDALKKTKKDDE HHCHHHHHHCCCCCH	61.18	-
147	Ubiquitination	VGTDALKKTKKDDEK HCHHHHHHCCCCCHH	67.44	-
147	Acetylation	VGTDALKKTKKDDEK HCHHHHHHCCCCCHH	67.44	7977183
158 (in isoform 2)	Ubiquitination	-	49.38	21890473
159	Sumoylation	DEKSKKSKEEYQQTW CHHHHHCHHHHHHHH	64.54	-
159 (in isoform 1)	Ubiquitination	-	64.54	21890473
159	Acetylation	DEKSKKSKEEYQQTW CHHHHHCHHHHHHHH	64.54	26051181
159	Ubiquitination	DEKSKKSKEEYQQTW CHHHHHCHHHHHHHH	64.54	21890473
159	Sumoylation	DEKSKKSKEEYQQTW CHHHHHCHHHHHHHH	64.54	-
162	Phosphorylation	SKKSKEEYQQTWYHE HHHCHHHHHHHHCCC	13.65	-
184	Phosphorylation	ARLWIANYSLPRAMK HHHHHHCCCHHHHHH	11.54	23186163
185	Phosphorylation	RLWIANYSLPRAMKR HHHHHCCCHHHHHHH	31.53	23186163
200	Ubiquitination	LEEARLHKEIPETTR HHHHHHHCCCCCCCC	63.03	-
216	Ubiquitination	SQMQELHKSLRSLNN HHHHHHHHHHHHHHH	64.90	-
236	Phosphorylation	GDDRPISYCHFSPNS CCCCCCCCCEECCCC	7.23	20873877
240	Phosphorylation	PISYCHFSPNSKMLA CCCCCEECCCCHHHH	10.25	25159151
244	Acetylation	CHFSPNSKMLATACW CEECCCCHHHHHHHH	44.57	26051181
284	Ubiquitination	GAIVFHPKSTVSLDP EEEEECCCCCCCCCH	50.63	-
284	Acetylation	GAIVFHPKSTVSLDP EEEEECCCCCCCCCH	50.63	26051181
292	Ubiquitination	STVSLDPKDVNLASC CCCCCCHHHCCCHHH	74.17	-
292	Acetylation	STVSLDPKDVNLASC CCCCCCHHHCCCHHH	74.17	26051181
306	Acetylation	CAADGSVKLWSLDSD HHCCCCEEEEECCCC	46.03	26051181
345	Methylation	LGTTCYDRSWRLWDL CCCEEECCCEEEECH	16.19	115488999
432	Acetylation	GSGDNTCKVWDLRQR CCCCCCEEEEECCCC	44.30	26051181
456	Acetylation	QNLVTGVKFEPIHGN CCCCCCCEEEECCCC	45.41	30591567
478	Phosphorylation	DNTAKIWTHPGWSPL CCCCEEEECCCCCCC	22.97	28152594
483	Phosphorylation	IWTHPGWSPLKTLAG EEECCCCCCCHHHCC	26.69	25159151
486	Acetylation	HPGWSPLKTLAGHEG CCCCCCCHHHCCCCC	44.89	26051181
486	Ubiquitination	HPGWSPLKTLAGHEG CCCCCCCHHHCCCCC	44.89	-
487	Phosphorylation	PGWSPLKTLAGHEGK CCCCCCHHHCCCCCE	29.53	22210691
511	Phosphorylation	GQLIATCSYDRTFKL CCEEEEEECCCEEEE	26.22	22210691
512	Phosphorylation	QLIATCSYDRTFKLW CEEEEEECCCEEEEE	16.16	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 PRP4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PRP4_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 PRP4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PFD1_HUMAN	PFDN1	physical	19615732
PFD4_HUMAN	PFDN4	physical	19615732
PFD5_HUMAN	PFDN5	physical	19615732
PFD3_HUMAN	VBP1	physical	19615732
PRP4B_HUMAN	PRPF4B	physical	19615732
SNUT1_HUMAN	SART1	physical	19615732
PRPF3_HUMAN	PRPF3	physical	19615732
SNR40_HUMAN	SNRNP40	physical	19615732
DDX23_HUMAN	DDX23	physical	19615732
GEPH_HUMAN	GPHN	physical	19615732
N42L2_HUMAN	N4BP2L2	physical	19615732
PPIH_HUMAN	PPIH	physical	19615732
PFD6_HUMAN	PFDN6	physical	19615732
PRP8_HUMAN	PRPF8	physical	19615732
SNUT2_HUMAN	USP39	physical	19615732
KDM5B_HUMAN	KDM5B	physical	19615732
TXN4A_HUMAN	TXNL4A	physical	19615732
SNR27_HUMAN	SNRNP27	physical	19615732
LSM6_HUMAN	LSM6	physical	19615732
PRP6_HUMAN	PRPF6	physical	19615732
LSM4_HUMAN	LSM4	physical	19615732
PRP31_HUMAN	PRPF31	physical	19615732
LSM7_HUMAN	LSM7	physical	19615732
LSM8_HUMAN	LSM8	physical	19615732
MEPCE_HUMAN	MEPCE	physical	19615732
LSM2_HUMAN	LSM2	physical	19615732
STPAP_HUMAN	TUT1	physical	19615732
RBM42_HUMAN	RBM42	physical	19615732
UBP15_HUMAN	USP15	physical	19615732
NH2L1_HUMAN	NHP2L1	physical	16723661
PPIH_HUMAN	PPIH	physical	16723661
PRPF3_HUMAN	PRPF3	physical	16723661
PRP4_HUMAN	PRPF4	physical	16723661
PRP31_HUMAN	PRPF31	physical	16723661
A4_HUMAN	APP	physical	21832049
PRPF3_HUMAN	PRPF3	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
RU2B_HUMAN	SNRPB2	physical	22939629
RS10_HUMAN	RPS10	physical	22939629
WAP53_HUMAN	WRAP53	physical	22939629
TXND5_HUMAN	TXNDC5	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22365833
PPIH_HUMAN	PPIH	physical	22365833
GPKOW_HUMAN	GPKOW	physical	22365833
SRSF1_HUMAN	SRSF1	physical	15452250
DDX23_HUMAN	DDX23	physical	26344197
DHX37_HUMAN	DHX37	physical	26344197
LKHA4_HUMAN	LTA4H	physical	26344197
PRP8_HUMAN	PRPF8	physical	26344197
SNUT1_HUMAN	SART1	physical	26344197
SF3A1_HUMAN	SF3A1	physical	26344197
U520_HUMAN	SNRNP200	physical	26344197
ARBK1_HUMAN	ADRBK1	physical	26496610
TCPZ_HUMAN	CCT6A	physical	26496610
DPH1_HUMAN	DPH1	physical	26496610
LG3BP_HUMAN	LGALS3BP	physical	26496610
LIFR_HUMAN	LIFR	physical	26496610
PRIC3_HUMAN	PRICKLE3	physical	26496610
IKBE_HUMAN	NFKBIE	physical	26496610
NH2L1_HUMAN	NHP2L1	physical	26496610
TCPA_HUMAN	TCP1	physical	26496610
TCPG_HUMAN	CCT3	physical	26496610
SNUT1_HUMAN	SART1	physical	26496610
PRPF3_HUMAN	PRPF3	physical	26496610
DDX23_HUMAN	DDX23	physical	26496610
CAPON_HUMAN	NOS1AP	physical	26496610
SART3_HUMAN	SART3	physical	26496610
GEPH_HUMAN	GPHN	physical	26496610
TCPH_HUMAN	CCT7	physical	26496610
TCPD_HUMAN	CCT4	physical	26496610
TCPB_HUMAN	CCT2	physical	26496610
PRP8_HUMAN	PRPF8	physical	26496610
TCPQ_HUMAN	CCT8	physical	26496610
SNUT2_HUMAN	USP39	physical	26496610
RPP29_HUMAN	POP4	physical	26496610
CSN5_HUMAN	COPS5	physical	26496610
CDC37_HUMAN	CDC37	physical	26496610
TCPE_HUMAN	CCT5	physical	26496610
U520_HUMAN	SNRNP200	physical	26496610
SYNE2_HUMAN	SYNE2	physical	26496610
FKB15_HUMAN	FKBP15	physical	26496610
PRP6_HUMAN	PRPF6	physical	26496610
PRP31_HUMAN	PRPF31	physical	26496610
NARF_HUMAN	NARF	physical	26496610
ABT1_HUMAN	ABT1	physical	26496610
OTUD4_HUMAN	OTUD4	physical	26496610
ENAH_HUMAN	ENAH	physical	26496610
DHX33_HUMAN	DHX33	physical	26496610
ERGI1_HUMAN	ERGIC1	physical	26496610
ZGPAT_HUMAN	ZGPAT	physical	26496610
ACBD5_HUMAN	ACBD5	physical	26496610
TOE1_HUMAN	TOE1	physical	26496610
AGAP1_HUMAN	AGAP1	physical	26496610
PTGR2_HUMAN	PTGR2	physical	26496610
SAS6_HUMAN	SASS6	physical	26496610
CCD84_HUMAN	CCDC84	physical	26496610
SART3_HUMAN	SART3	physical	28514442
STPAP_HUMAN	TUT1	physical	28514442
GEPH_HUMAN	GPHN	physical	28514442
N42L2_HUMAN	N4BP2L2	physical	28514442
SMD2_HUMAN	SNRPD2	physical	28514442
NH2L1_HUMAN	NHP2L1	physical	28514442
PRP6_HUMAN	PRPF6	physical	28514442
LSM8_HUMAN	LSM8	physical	28514442
LSM4_HUMAN	LSM4	physical	28514442
U520_HUMAN	SNRNP200	physical	28514442
THOC4_HUMAN	ALYREF	physical	27173435
LSM8_HUMAN	LSM8	physical	27173435
LSM4_HUMAN	LSM4	physical	27173435
SART3_HUMAN	SART3	physical	27173435
RL26L_HUMAN	RPL26L1	physical	27173435
OLA1_HUMAN	OLA1	physical	27173435
RL32_HUMAN	RPL32	physical	27173435
LSM6_HUMAN	LSM6	physical	27173435
RINI_HUMAN	RNH1	physical	27173435
CHCH2_HUMAN	CHCHD2	physical	27173435
UBIM_HUMAN	FAU	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615922	Retinitis pigmentosa 70 (RP70)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PRP4_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-27, AND MASS SPECTROMETRY.	19608861 [Abstract]