dbPTM

RED_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RED_HUMAN
UniProt AC	Q13123
Protein Name	Protein Red {ECO:0000303\|PubMed:10216252}
Gene Name	IK
Organism	Homo sapiens (Human).
Sequence Length	557
Subcellular Localization	Nucleus . Nucleus, nucleoplasm . Chromosome . Cytoplasm, cytoskeleton, spindle pole . Predominantly present throughout the nucleoplasm during prometaphase, metaphase and anaphase. Is also detected in nuclear foci that are not identical with Cajal bod
Protein Description	Involved in pre-mRNA splicing as a component of the spliceosome. [PubMed: 28781166 Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species (Probable Required for normal mitotic cell cycle progression]
Protein Sequence	MPERDSEPFSNPLAPDGHDVDDPHSFHQSKLTNEDFRKLLMTPRAAPTSAPPSKSRHHEMPREYNEDEDPAARRRKKKSYYAKLRQQEIERERELAEKYRDRAKERRDGVNKDYEETELISTTANYRAVGPTAEADKSAAEKRRQLIQESKFLGGDMEHTHLVKGLDFALLQKVRAEIASKEKEEEELMEKPQKETKKDEDPENKIEFKTRLGRNVYRMLFKSKAYERNELFLPGRMAYVVDLDDEYADTDIPTTLIRSKADCPTMEAQTTLTTNDIVISKLTQILSYLRQGTRNKKLKKKDKGKLEEKKPPEADMNIFEDIGDYVPSTTKTPRDKERERYRERERDRERDRDRDRERERERDRERERERDREREEEKKRHSYFEKPKVDDEPMDVDKGPGSTKELIKSINEKFAGSAGWEGTESLKKPEDKKQLGDFFGMSNSYAECYPATMDDMAVDSDEEVDYSKMDQGNKKGPLGRWDFDTQEEYSEYMNNKEALPKAAFQYGIKMSEGRKTRRFKETNDKAELDRQWKKISAIIEKRKKMEADGVEVKRPKY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MPERDSEPFSNPL --CCCCCCCCCCCCC	54.08	20068231
10	Phosphorylation	ERDSEPFSNPLAPDG CCCCCCCCCCCCCCC	48.53	20068231
25	Phosphorylation	HDVDDPHSFHQSKLT CCCCCCCCCHHHHCC	29.79	23186163
29	Phosphorylation	DPHSFHQSKLTNEDF CCCCCHHHHCCHHHH	22.51	23186163
30	Ubiquitination	PHSFHQSKLTNEDFR CCCCHHHHCCHHHHH	53.40	-
38	Sumoylation	LTNEDFRKLLMTPRA CCHHHHHHHHCCCCC	46.06	-
38	Sumoylation	LTNEDFRKLLMTPRA CCHHHHHHHHCCCCC	46.06	-
38	Ubiquitination	LTNEDFRKLLMTPRA CCHHHHHHHHCCCCC	46.06	-
42	Phosphorylation	DFRKLLMTPRAAPTS HHHHHHCCCCCCCCC	15.02	21712546
48	Phosphorylation	MTPRAAPTSAPPSKS CCCCCCCCCCCCCCC	32.56	20068231
49	Phosphorylation	TPRAAPTSAPPSKSR CCCCCCCCCCCCCCC	37.41	25159151
53	Phosphorylation	APTSAPPSKSRHHEM CCCCCCCCCCCCCCC	42.05	28634298
54	Acetylation	PTSAPPSKSRHHEMP CCCCCCCCCCCCCCC	58.23	24886839
54	Ubiquitination	PTSAPPSKSRHHEMP CCCCCCCCCCCCCCC	58.23	-
55	Phosphorylation	TSAPPSKSRHHEMPR CCCCCCCCCCCCCCC	40.98	28634298
83	Acetylation	KKKSYYAKLRQQEIE HHHHHHHHHHHHHHH	28.25	19608861
83	Ubiquitination	KKKSYYAKLRQQEIE HHHHHHHHHHHHHHH	28.25	19608861
98	Acetylation	RERELAEKYRDRAKE HHHHHHHHHHHHHHH	39.72	19608861
98	Ubiquitination	RERELAEKYRDRAKE HHHHHHHHHHHHHHH	39.72	19608861
112	Ubiquitination	ERRDGVNKDYEETEL HHHCCCCCCHHHHHH	60.32	-
114	Phosphorylation	RDGVNKDYEETELIS HCCCCCCHHHHHHHE	19.78	28796482
117	Phosphorylation	VNKDYEETELISTTA CCCCHHHHHHHEEEC	24.93	28796482
121	Phosphorylation	YEETELISTTANYRA HHHHHHHEEECCCEE	32.12	28060719
122	Phosphorylation	EETELISTTANYRAV HHHHHHEEECCCEEC	23.96	28060719
123	Phosphorylation	ETELISTTANYRAVG HHHHHEEECCCEECC	13.20	28060719
126	Phosphorylation	LISTTANYRAVGPTA HHEEECCCEECCCCH	9.48	28796482
137	Acetylation	GPTAEADKSAAEKRR CCCHHHCHHHHHHHH	49.38	23749302
138	Phosphorylation	PTAEADKSAAEKRRQ CCHHHCHHHHHHHHH	33.00	21712546
142	Ubiquitination	ADKSAAEKRRQLIQE HCHHHHHHHHHHHHH	48.42	-
151	Sumoylation	RQLIQESKFLGGDME HHHHHHHHCCCCCCC	43.80	-
151	Sumoylation	RQLIQESKFLGGDME HHHHHHHHCCCCCCC	43.80	28112733
151	Ubiquitination	RQLIQESKFLGGDME HHHHHHHHCCCCCCC	43.80	-
164	Ubiquitination	MEHTHLVKGLDFALL CCHHHHHCCHHHHHH	61.18	-
173	Sumoylation	LDFALLQKVRAEIAS HHHHHHHHHHHHHHC	33.39	-
173	2-Hydroxyisobutyrylation	LDFALLQKVRAEIAS HHHHHHHHHHHHHHC	33.39	-
173	Sumoylation	LDFALLQKVRAEIAS HHHHHHHHHHHHHHC	33.39	-
173	Ubiquitination	LDFALLQKVRAEIAS HHHHHHHHHHHHHHC	33.39	21890473
173	Ubiquitination	LDFALLQKVRAEIAS HHHHHHHHHHHHHHC	33.39	21890473
191	Acetylation	EEEELMEKPQKETKK HHHHHHHHCCHHCCC	38.49	26051181
191	Ubiquitination	EEEELMEKPQKETKK HHHHHHHHCCHHCCC	38.49	2190698
198	Ubiquitination	KPQKETKKDEDPENK HCCHHCCCCCCCCHH	74.00	-
205	Sumoylation	KDEDPENKIEFKTRL CCCCCCHHHHHHHHH	41.78	-
205	Sumoylation	KDEDPENKIEFKTRL CCCCCCHHHHHHHHH	41.78	-
205	Ubiquitination	KDEDPENKIEFKTRL CCCCCCHHHHHHHHH	41.78	-
209	Ubiquitination	PENKIEFKTRLGRNV CCHHHHHHHHHCHHH	21.68	-
224	Sumoylation	YRMLFKSKAYERNEL HHHHHCCCCHHCCCC	56.42	-
224	Sumoylation	YRMLFKSKAYERNEL HHHHHCCCCHHCCCC	56.42	-
247	Phosphorylation	VVDLDDEYADTDIPT EEECCHHHCCCCCCH	19.44	27642862
260	Acetylation	PTTLIRSKADCPTME CHHHHHCCCCCCCCC	38.09	26051181
260	Ubiquitination	PTTLIRSKADCPTME CHHHHHCCCCCCCCC	38.09	-
270	Phosphorylation	CPTMEAQTTLTTNDI CCCCCCCCCCCCHHH	30.71	28387310
271	Phosphorylation	PTMEAQTTLTTNDIV CCCCCCCCCCCHHHH	15.27	28387310
280	Phosphorylation	TTNDIVISKLTQILS CCHHHHHHHHHHHHH	15.66	28387310
283	Phosphorylation	DIVISKLTQILSYLR HHHHHHHHHHHHHHH	19.80	23186163
287	Phosphorylation	SKLTQILSYLRQGTR HHHHHHHHHHHHCCC	24.61	20873877
288	Phosphorylation	KLTQILSYLRQGTRN HHHHHHHHHHHCCCC	11.49	23186163
303	Acetylation	KKLKKKDKGKLEEKK HHCCCCCCCCCCCCC	67.82	7964201
305	Acetylation	LKKKDKGKLEEKKPP CCCCCCCCCCCCCCC	59.47	7964211
310	Sumoylation	KGKLEEKKPPEADMN CCCCCCCCCCHHHCC	69.91	-
310	Sumoylation	KGKLEEKKPPEADMN CCCCCCCCCCHHHCC	69.91	28112733
310	Ubiquitination	KGKLEEKKPPEADMN CCCCCCCCCCHHHCC	69.91	-
325	Phosphorylation	IFEDIGDYVPSTTKT HHHHHHHCCCCCCCC	14.73	18669648
328	Phosphorylation	DIGDYVPSTTKTPRD HHHHCCCCCCCCCCH	38.37	25159151
329	Phosphorylation	IGDYVPSTTKTPRDK HHHCCCCCCCCCCHH	26.66	29978859
330	Phosphorylation	GDYVPSTTKTPRDKE HHCCCCCCCCCCHHH	36.94	25159151
331	Sumoylation	DYVPSTTKTPRDKER HCCCCCCCCCCHHHH	57.53	28112733
331	Ubiquitination	DYVPSTTKTPRDKER HCCCCCCCCCCHHHH	57.53	-
332	Phosphorylation	YVPSTTKTPRDKERE CCCCCCCCCCHHHHH	22.82	21712546
382	Phosphorylation	EEEKKRHSYFEKPKV HHHHHHHHCCCCCCC	35.23	27251275
383	Phosphorylation	EEKKRHSYFEKPKVD HHHHHHHCCCCCCCC	15.05	-
386	Acetylation	KRHSYFEKPKVDDEP HHHHCCCCCCCCCCC	39.99	19608861
386	Sumoylation	KRHSYFEKPKVDDEP HHHHCCCCCCCCCCC	39.99	28112733
388	Sumoylation	HSYFEKPKVDDEPMD HHCCCCCCCCCCCCC	70.17	-
388	Sumoylation	HSYFEKPKVDDEPMD HHCCCCCCCCCCCCC	70.17	28112733
394	Sulfoxidation	PKVDDEPMDVDKGPG CCCCCCCCCCCCCCC	8.04	21406390
398	Acetylation	DEPMDVDKGPGSTKE CCCCCCCCCCCCHHH	67.84	26051181
402	Phosphorylation	DVDKGPGSTKELIKS CCCCCCCCHHHHHHH	39.17	30576142
403	Phosphorylation	VDKGPGSTKELIKSI CCCCCCCHHHHHHHH	34.16	30576142
404	Sumoylation	DKGPGSTKELIKSIN CCCCCCHHHHHHHHH	52.82	-
404	Sumoylation	DKGPGSTKELIKSIN CCCCCCHHHHHHHHH	52.82	28112733
404	Ubiquitination	DKGPGSTKELIKSIN CCCCCCHHHHHHHHH	52.82	-
408	Sumoylation	GSTKELIKSINEKFA CCHHHHHHHHHHHHC	58.89	-
408	Acetylation	GSTKELIKSINEKFA CCHHHHHHHHHHHHC	58.89	19608861
408	Sumoylation	GSTKELIKSINEKFA CCHHHHHHHHHHHHC	58.89	28112733
408	Ubiquitination	GSTKELIKSINEKFA CCHHHHHHHHHHHHC	58.89	19608861
409	Phosphorylation	STKELIKSINEKFAG CHHHHHHHHHHHHCC	24.53	30108239
413	Sumoylation	LIKSINEKFAGSAGW HHHHHHHHHCCCCCC	35.71	-
413	Sumoylation	LIKSINEKFAGSAGW HHHHHHHHHCCCCCC	35.71	-
413	Ubiquitination	LIKSINEKFAGSAGW HHHHHHHHHCCCCCC	35.71	-
417	Phosphorylation	INEKFAGSAGWEGTE HHHHHCCCCCCCCHH	21.85	30108239
423	Phosphorylation	GSAGWEGTESLKKPE CCCCCCCHHHCCCHH	15.75	20068231
425	Phosphorylation	AGWEGTESLKKPEDK CCCCCHHHCCCHHHH	45.38	23186163
442	Phosphorylation	LGDFFGMSNSYAECY HHHHHCCCCCHHHHE	24.01	27251275
444	Phosphorylation	DFFGMSNSYAECYPA HHHCCCCCHHHHEEC	20.57	27251275
445	Phosphorylation	FFGMSNSYAECYPAT HHCCCCCHHHHEECC	15.63	26657352
449	Phosphorylation	SNSYAECYPATMDDM CCCHHHHEECCHHHC	6.34	26657352
452	Phosphorylation	YAECYPATMDDMAVD HHHHEECCHHHCCCC	19.34	18669648
460	Phosphorylation	MDDMAVDSDEEVDYS HHHCCCCCCCCCCHH	40.08	20058876
466	Phosphorylation	DSDEEVDYSKMDQGN CCCCCCCHHHCCCCC	18.50	26074081
467	Phosphorylation	SDEEVDYSKMDQGNK CCCCCCHHHCCCCCC	19.62	23090842
485	Phosphorylation	LGRWDFDTQEEYSEY CCCCCCCCHHHHHHH	37.56	17525332
489	Phosphorylation	DFDTQEEYSEYMNNK CCCCHHHHHHHHCCC	13.17	28796482
490	Phosphorylation	FDTQEEYSEYMNNKE CCCHHHHHHHHCCCC	26.07	28796482
492	Phosphorylation	TQEEYSEYMNNKEAL CHHHHHHHHCCCCHH	10.13	28796482
496	Sumoylation	YSEYMNNKEALPKAA HHHHHCCCCHHCHHH	39.08	28112733
501	Sumoylation	NNKEALPKAAFQYGI CCCCHHCHHHHHHCC	53.87	-
501	Sumoylation	NNKEALPKAAFQYGI CCCCHHCHHHHHHCC	53.87	28112733
501	Ubiquitination	NNKEALPKAAFQYGI CCCCHHCHHHHHHCC	53.87	-
506	Phosphorylation	LPKAAFQYGIKMSEG HCHHHHHHCCCCCCC	17.86	28152594
509	Sumoylation	AAFQYGIKMSEGRKT HHHHHCCCCCCCCCC	31.82	28112733
509	Ubiquitination	AAFQYGIKMSEGRKT HHHHHCCCCCCCCCC	31.82	-
516	Phosphorylation	KMSEGRKTRRFKETN CCCCCCCCCCCHHCC	26.22	22798277
520	Methylation	GRKTRRFKETNDKAE CCCCCCCHHCCCHHH	62.91	115971385
520	Ubiquitination	GRKTRRFKETNDKAE CCCCCCCHHCCCHHH	62.91	-
522	Phosphorylation	KTRRFKETNDKAELD CCCCCHHCCCHHHHH	49.67	23532336
530	Methylation	NDKAELDRQWKKISA CCHHHHHHHHHHHHH	57.81	115480229
534	Ubiquitination	ELDRQWKKISAIIEK HHHHHHHHHHHHHHH	38.65	-
536	Phosphorylation	DRQWKKISAIIEKRK HHHHHHHHHHHHHHH	23.46	28112733
541	2-Hydroxyisobutyrylation	KISAIIEKRKKMEAD HHHHHHHHHHHCCCC	60.14	-
541	Acetylation	KISAIIEKRKKMEAD HHHHHHHHHHHCCCC	60.14	25953088
541	Sumoylation	KISAIIEKRKKMEAD HHHHHHHHHHHCCCC	60.14	28112733
541	Ubiquitination	KISAIIEKRKKMEAD HHHHHHHHHHHCCCC	60.14	-
543	Sumoylation	SAIIEKRKKMEADGV HHHHHHHHHCCCCCC	68.49	28112733
544	Sumoylation	AIIEKRKKMEADGVE HHHHHHHHCCCCCCE	46.11	-
544	Sumoylation	AIIEKRKKMEADGVE HHHHHHHHCCCCCCE	46.11	28112733
553	Sumoylation	EADGVEVKRPKY--- CCCCCEECCCCC---	49.86	-
553	Acetylation	EADGVEVKRPKY--- CCCCCEECCCCC---	49.86	25953088
553	Sumoylation	EADGVEVKRPKY--- CCCCCEECCCCC---	49.86	28112733

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 RED_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PROF2_HUMAN	PFN2	physical	16169070
CHD3_HUMAN	CHD3	physical	16169070
KAT5_HUMAN	KAT5	physical	16169070
A4_HUMAN	APP	physical	21832049
SRS11_HUMAN	SRSF11	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
SRSF7_HUMAN	SRSF7	physical	22939629
U2AF2_HUMAN	U2AF2	physical	22939629
THOC1_HUMAN	THOC1	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
SAP18_HUMAN	SAP18	physical	22939629
TOP1_HUMAN	TOP1	physical	22939629
SEPT7_HUMAN	SEPT7	physical	22939629
SERA_HUMAN	PHGDH	physical	22939629
SRS10_HUMAN	SRSF10	physical	22939629
SMCA5_HUMAN	SMARCA5	physical	22939629
SP16H_HUMAN	SUPT16H	physical	22939629
TPR_HUMAN	TPR	physical	22939629
SRCAP_HUMAN	SRCAP	physical	22939629
TOP2B_HUMAN	TOP2B	physical	22939629
TR150_HUMAN	THRAP3	physical	22939629
RS7_HUMAN	RPS7	physical	22939629
WDR18_HUMAN	WDR18	physical	22939629
TRA2A_HUMAN	TRA2A	physical	22939629
SAFB2_HUMAN	SAFB2	physical	22939629
ZN326_HUMAN	ZNF326	physical	22939629
VTNC_HUMAN	VTN	physical	22939629
RBM10_HUMAN	RBM10	physical	22365833
U5S1_HUMAN	EFTUD2	physical	22365833
PRP6_HUMAN	PRPF6	physical	22365833
CTBL1_HUMAN	CTNNBL1	physical	22365833
SYF1_HUMAN	XAB2	physical	22365833
SNIP1_HUMAN	SNIP1	physical	22365833
MFAP1_HUMAN	MFAP1	physical	22365833
RED_HUMAN	IK	physical	22365833
SMU1_HUMAN	SMU1	physical	22365833
THOC1_HUMAN	THOC1	physical	22365833
F10C1_HUMAN	FRA10AC1	physical	22365833
ZN830_HUMAN	ZNF830	physical	22365833
TOE1_HUMAN	TOE1	physical	22365833
TTC14_HUMAN	TTC14	physical	22365833
ZCH10_HUMAN	ZCCHC10	physical	22365833
R113A_HUMAN	RNF113A	physical	22365833
RACK1_HUMAN	GNB2L1	physical	22365833
KDM1A_HUMAN	KDM1A	physical	23455924
CEP70_HUMAN	CEP70	physical	25416956

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 RED_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-83; LYS-98; LYS-386 ANDLYS-408, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND MASSSPECTROMETRY.	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-460, 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 THR-485, AND MASSSPECTROMETRY.	17525332 [Abstract]