dbPTM

CPSF5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CPSF5_HUMAN
UniProt AC	O43809
Protein Name	Cleavage and polyadenylation specificity factor subunit 5 {ECO:0000303\|PubMed:23187700}
Gene Name	NUDT21 {ECO:0000312\|HGNC:HGNC:13870}
Organism	Homo sapiens (Human).
Sequence Length	227
Subcellular Localization	Nucleus . Cytoplasm . Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460). In punctate subnuclear structures locali
Protein Description	Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. [PubMed: 9659921]
Protein Sequence	MSVVPPNRSQTGWPRGVTQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVVPPNRS ------CCCCCCCCC	31.64	-
2	Phosphorylation	------MSVVPPNRS ------CCCCCCCCC	31.64	27486199
8	Methylation	MSVVPPNRSQTGWPR CCCCCCCCCCCCCCC	35.60	-
9	Phosphorylation	SVVPPNRSQTGWPRG CCCCCCCCCCCCCCC	38.44	26699800
11	Phosphorylation	VPPNRSQTGWPRGVT CCCCCCCCCCCCCCC	42.32	26699800
15	Methylation	RSQTGWPRGVTQFGN CCCCCCCCCCCCCCH	45.78	24129315
18	Phosphorylation	TGWPRGVTQFGNKYI CCCCCCCCCCCHHEE	22.47	26699800
23	Methylation	GVTQFGNKYIQQTKP CCCCCCHHEECCCCC	44.07	17172643
23	Acetylation	GVTQFGNKYIQQTKP CCCCCCHHEECCCCC	44.07	17172643
23	Ubiquitination	GVTQFGNKYIQQTKP CCCCCCHHEECCCCC	44.07	21906983
23	2-Hydroxyisobutyrylation	GVTQFGNKYIQQTKP CCCCCCHHEECCCCC	44.07	-
24	Phosphorylation	VTQFGNKYIQQTKPL CCCCCHHEECCCCCE	14.15	28152594
28	Phosphorylation	GNKYIQQTKPLTLER CHHEECCCCCEEEEE	20.46	26699800
29	Malonylation	NKYIQQTKPLTLERT HHEECCCCCEEEEEE	33.42	26320211
29	Acetylation	NKYIQQTKPLTLERT HHEECCCCCEEEEEE	33.42	19608861
29	Ubiquitination	NKYIQQTKPLTLERT HHEECCCCCEEEEEE	33.42	21890473
36	Phosphorylation	KPLTLERTINLYPLT CCEEEEEEEEEEECC	12.58	-
40	Phosphorylation	LERTINLYPLTNYTF EEEEEEEEECCCCCC	7.54	20090780
43	Phosphorylation	TINLYPLTNYTFGTK EEEEEECCCCCCCCC	22.98	28152594
45	Phosphorylation	NLYPLTNYTFGTKEP EEEECCCCCCCCCCC	9.75	-
46	Phosphorylation	LYPLTNYTFGTKEPL EEECCCCCCCCCCCC	20.05	29496907
49	Phosphorylation	LTNYTFGTKEPLYEK CCCCCCCCCCCCCCC	28.22	-
50	Ubiquitination	TNYTFGTKEPLYEKD CCCCCCCCCCCCCCC	58.68	21906983
54	Phosphorylation	FGTKEPLYEKDSSVA CCCCCCCCCCCHHHH	31.48	29496907
56	Acetylation	TKEPLYEKDSSVAAR CCCCCCCCCHHHHHH	49.72	19608861
56	Ubiquitination	TKEPLYEKDSSVAAR CCCCCCCCCHHHHHH	49.72	21906983
56	2-Hydroxyisobutyrylation	TKEPLYEKDSSVAAR CCCCCCCCCHHHHHH	49.72	-
73	Ubiquitination	RMREEFDKIGMRRTV HHHHHHHHHCCCCCE	46.62	19608861
73	Acetylation	RMREEFDKIGMRRTV HHHHHHHHHCCCCCE	46.62	19608861
101	Phosphorylation	VLLLQLGTTFFKLPG EEEEECCCCEEECCC	29.08	20068231
102	Phosphorylation	LLLQLGTTFFKLPGG EEEECCCCEEECCCC	25.85	20068231
122	Ubiquitination	EDEVEGLKRLMTEIL CHHHHHHHHHHHHHH	55.10	21906983
122	2-Hydroxyisobutyrylation	EDEVEGLKRLMTEIL CHHHHHHHHHHHHHH	55.10	-
122	Acetylation	EDEVEGLKRLMTEIL CHHHHHHHHHHHHHH	55.10	26051181
125	Sulfoxidation	VEGLKRLMTEILGRQ HHHHHHHHHHHHCCC	3.52	21406390
126	Phosphorylation	EGLKRLMTEILGRQD HHHHHHHHHHHCCCC	25.19	28851738
182	Ubiquitination	FLVQLQEKALFAVPK EEEEHHHHHHHCCCC	37.11	21906983
189	Ubiquitination	KALFAVPKNYKLVAA HHHHCCCCCCEEEEE	67.33	21890473
189	Malonylation	KALFAVPKNYKLVAA HHHHCCCCCCEEEEE	67.33	26320211
189	Acetylation	KALFAVPKNYKLVAA HHHHCCCCCCEEEEE	67.33	19608861
192	Ubiquitination	FAVPKNYKLVAAPLF HCCCCCCEEEEEEHH	45.97	-
226	Phosphorylation	LSRFNFIYN------ HHHCCCCCC------	15.64	25839225

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 CPSF5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CPSF5_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 CPSF5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NIF3L_HUMAN	NIF3L1	physical	16189514
CPSF7_HUMAN	CPSF7	physical	16189514
CPSF6_HUMAN	CPSF6	physical	16189514
CPSF5_HUMAN	NUDT21	physical	16189514
RBM48_HUMAN	RBM48	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
RLA1_HUMAN	RPLP1	physical	16169070
HDAC1_HUMAN	HDAC1	physical	17172643
HDAC3_HUMAN	HDAC3	physical	17172643
HDA10_HUMAN	HDAC10	physical	17172643
SIR1_HUMAN	SIRT1	physical	17172643
SIR2_HUMAN	SIRT2	physical	17172643
DNM3L_HUMAN	DNMT3L	physical	21900206
FUND2_HUMAN	FUNDC2	physical	21900206
SF3B1_HUMAN	SF3B1	physical	21900206
A2MG_HUMAN	A2M	physical	21900206
CE126_HUMAN	KIAA1377	physical	21900206
EF1G_HUMAN	EEF1G	physical	21900206
DC1I1_HUMAN	DYNC1I1	physical	21900206
EED_HUMAN	EED	physical	21900206
FBN3_HUMAN	FBN3	physical	21900206
FAD1_HUMAN	FLAD1	physical	21900206
SHC1_HUMAN	SHC1	physical	21900206
CTL1_HUMAN	SLC44A1	physical	21900206
KIFA3_HUMAN	KIFAP3	physical	21900206
SEM5B_HUMAN	SEMA5B	physical	21900206
RN19A_HUMAN	RNF19A	physical	21900206
RBM48_HUMAN	RBM48	physical	21900206
DREB_HUMAN	DBN1	physical	21900206
TZAP_HUMAN	ZBTB48	physical	21900206
TRA2A_HUMAN	TRA2A	physical	21900206
JHD2C_HUMAN	JMJD1C	physical	21900206
F13A_HUMAN	F13A1	physical	21900206
P5CR1_HUMAN	PYCR1	physical	21900206
RPB3_HUMAN	POLR2C	physical	21900206
HSF4_HUMAN	HSF4	physical	21900206
RCC1_HUMAN	RCC1	physical	21900206
SEM1_HUMAN	SHFM1	physical	21900206
RLA1_HUMAN	RPLP1	physical	21900206
TLE1_HUMAN	TLE1	physical	21900206
IKZF1_HUMAN	IKZF1	physical	21900206
MASP1_HUMAN	MASP1	physical	21900206
SNCAP_HUMAN	SNCAIP	physical	21900206
CTND2_HUMAN	CTNND2	physical	21900206
PTN_HUMAN	PTN	physical	21900206
NGEF_HUMAN	NGEF	physical	21900206
CPSF6_HUMAN	CPSF6	physical	22939629
SK2L2_HUMAN	SKIV2L2	physical	22939629
XRCC4_HUMAN	XRCC4	physical	22939629
IF4H_HUMAN	EIF4H	physical	22939629
SI1L1_HUMAN	SIPA1L1	physical	22939629
FAF1_HUMAN	FAF1	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
VIME_HUMAN	VIM	physical	22939629
S10AD_HUMAN	S100A13	physical	22939629
SELB_HUMAN	EEFSEC	physical	22939629
HDAC2_HUMAN	HDAC2	physical	22939629
CARM1_HUMAN	CARM1	physical	23455924
CPSF5_HUMAN	NUDT21	physical	25416956
CPSF7_HUMAN	CPSF7	physical	25416956
LMAN1_HUMAN	LMAN1	physical	26344197
LRC47_HUMAN	LRRC47	physical	26344197
PCF11_HUMAN	PCF11	physical	26344197
TZAP_HUMAN	ZBTB48	physical	26496610
NUP98_HUMAN	NUP98	physical	26496610
TOP3B_HUMAN	TOP3B	physical	26496610
CRTAP_HUMAN	CRTAP	physical	26496610
CPSF6_HUMAN	CPSF6	physical	26496610
P3H2_HUMAN	P3H2	physical	26496610
P3H1_HUMAN	P3H1	physical	26496610
CPSF7_HUMAN	CPSF7	physical	26496610

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 CPSF5_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-23; LYS-29; LYS-56; LYS-73AND LYS-189, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Multiple histone deacetylases and the CREB-binding protein regulatepre-mRNA 3'-end processing."; Shimazu T., Horinouchi S., Yoshida M.; J. Biol. Chem. 282:4470-4478(2007). Cited for: ACETYLATION AT LYS-23, INTERACTION WITH PAPOLA AND CPSF6, MASSSPECTROMETRY, AND MUTAGENESIS OF LYS-23 AND LYS-29.	17172643 [Abstract]
Phosphorylation
Reference	PubMed
"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-40, AND MASSSPECTROMETRY.	15592455 [Abstract]