dbPTM

CNOT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CNOT2_HUMAN
UniProt AC	Q9NZN8
Protein Name	CCR4-NOT transcription complex subunit 2
Gene Name	CNOT2
Organism	Homo sapiens (Human).
Sequence Length	540
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for the CCR4-NOT complex structural integrity. Can repress transcription and may link the CCR4-NOT complex to transcriptional regulation; the repressive function may specifically involve the N-Cor repressor complex containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of emryonic stem (ES) cell identity..
Protein Sequence	MVRTDGHTLSEKRNYQVTNSMFGASRKKFVEGVDSDYHDENMYYSQSSMFPHRSEKDMLASPSTSGQLSQFGASLYGQQSALGLPMRGMSNNTPQLNRSLSQGTQLPSHVTPTTGVPTMSLHTPPSPSRGILPMNPRNMMNHSQVGQGIGIPSRTNSMSSSGLGSPNRSSPSIICMPKQQPSRQPFTVNSMSGFGMNRNQAFGMNNSLSSNIFNGTDGSENVTGLDLSDFPALADRNRREGSGNPTPLINPLAGRAPYVGMVTKPANEQSQDFSIHNEDFPALPGSSYKDPTSSNDDSKSNLNTSGKTTSSTDGPKFPGDKSSTTQNNNQQKKGIQVLPDGRVTNIPQGMVTDQFGMIGLLTFIRAAETDPGMVHLALGSDLTTLGLNLNSPENLYPKFASPWASSPCRPQDIDFHVPSEYLTNIHIRDKLAAIKLGRYGEDLLFYLYYMNGGDVLQLLAAVELFNRDWRYHKEERVWITRAPGMEPTMKTNTYERGTYYFFDCLNWRKVAKEFHLEYDKLEERPHLPSTFNYNPAQQAF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Ubiquitination	DGHTLSEKRNYQVTN CCCCCCCCCCHHHHH	42.44	-
15	Phosphorylation	TLSEKRNYQVTNSMF CCCCCCCHHHHHHCC	14.37	27642862
20	Phosphorylation	RNYQVTNSMFGASRK CCHHHHHHCCCCCHH	13.21	28555341
35	Phosphorylation	KFVEGVDSDYHDENM HHHHCCCCCCCCCCC	37.35	28796482
37	Phosphorylation	VEGVDSDYHDENMYY HHCCCCCCCCCCCCC	18.34	28796482
43	Phosphorylation	DYHDENMYYSQSSMF CCCCCCCCCCCCCCC	16.14	28796482
44	Phosphorylation	YHDENMYYSQSSMFP CCCCCCCCCCCCCCC	6.89	28796482
45	Phosphorylation	HDENMYYSQSSMFPH CCCCCCCCCCCCCCC	13.19	28796482
47	Phosphorylation	ENMYYSQSSMFPHRS CCCCCCCCCCCCCCC	20.17	28796482
48	Phosphorylation	NMYYSQSSMFPHRSE CCCCCCCCCCCCCCH	19.46	28796482
54	Phosphorylation	SSMFPHRSEKDMLAS CCCCCCCCHHHCCCC	46.06	27251275
56	Acetylation	MFPHRSEKDMLASPS CCCCCCHHHCCCCCC	50.08	7467815
61	Phosphorylation	SEKDMLASPSTSGQL CHHHCCCCCCCCHHH	18.54	28450419
63	Phosphorylation	KDMLASPSTSGQLSQ HHCCCCCCCCHHHHH	32.48	28450419
64	Phosphorylation	DMLASPSTSGQLSQF HCCCCCCCCHHHHHH	40.02	28450419
65	Phosphorylation	MLASPSTSGQLSQFG CCCCCCCCHHHHHHC	28.95	28450419
69	Phosphorylation	PSTSGQLSQFGASLY CCCCHHHHHHCHHHH	18.64	28450419
74	Phosphorylation	QLSQFGASLYGQQSA HHHHHCHHHHHHHHC	23.62	27080861
76	Phosphorylation	SQFGASLYGQQSALG HHHCHHHHHHHHCCC	15.47	27080861
80	Phosphorylation	ASLYGQQSALGLPMR HHHHHHHHCCCCCCC	19.99	27080861
87	Methylation	SALGLPMRGMSNNTP HCCCCCCCCCCCCCH	35.40	115389015
89	Sulfoxidation	LGLPMRGMSNNTPQL CCCCCCCCCCCCHHH	2.46	21406390
90	Phosphorylation	GLPMRGMSNNTPQLN CCCCCCCCCCCHHHH	29.74	30243723
93	Phosphorylation	MRGMSNNTPQLNRSL CCCCCCCCHHHHHHH	19.36	29255136
99	Phosphorylation	NTPQLNRSLSQGTQL CCHHHHHHHHCCCCC	31.16	26055452
101	Phosphorylation	PQLNRSLSQGTQLPS HHHHHHHHCCCCCCC	28.01	17525332
104	Phosphorylation	NRSLSQGTQLPSHVT HHHHHCCCCCCCCCC	21.21	28450419
108	Phosphorylation	SQGTQLPSHVTPTTG HCCCCCCCCCCCCCC	38.90	28450419
111	Phosphorylation	TQLPSHVTPTTGVPT CCCCCCCCCCCCCCC	14.97	21712546
113	O-linked_Glycosylation	LPSHVTPTTGVPTMS CCCCCCCCCCCCCEE	27.15	30059200
113	Phosphorylation	LPSHVTPTTGVPTMS CCCCCCCCCCCCCEE	27.15	25394399
114	Phosphorylation	PSHVTPTTGVPTMSL CCCCCCCCCCCCEEC	37.07	28450419
118	Phosphorylation	TPTTGVPTMSLHTPP CCCCCCCCEECCCCC	19.58	21082442
120	Phosphorylation	TTGVPTMSLHTPPSP CCCCCCEECCCCCCC	21.34	21712546
123	Phosphorylation	VPTMSLHTPPSPSRG CCCEECCCCCCCCCC	42.03	26055452
126	Phosphorylation	MSLHTPPSPSRGILP EECCCCCCCCCCCCC	36.39	26055452
128	Phosphorylation	LHTPPSPSRGILPMN CCCCCCCCCCCCCCC	47.69	30177828
137	Methylation	GILPMNPRNMMNHSQ CCCCCCHHHCCCHHH	38.38	115485459
141 (in isoform 3)	Ubiquitination	-	22.38	21906983
143	Phosphorylation	PRNMMNHSQVGQGIG HHHCCCHHHCCCCCC	22.89	28857561
155	Phosphorylation	GIGIPSRTNSMSSSG CCCCCCCCCCCCCCC	35.66	23927012
157	Phosphorylation	GIPSRTNSMSSSGLG CCCCCCCCCCCCCCC	21.30	23401153
159	Phosphorylation	PSRTNSMSSSGLGSP CCCCCCCCCCCCCCC	22.60	23927012
160	Phosphorylation	SRTNSMSSSGLGSPN CCCCCCCCCCCCCCC	21.56	23401153
161	Phosphorylation	RTNSMSSSGLGSPNR CCCCCCCCCCCCCCC	30.63	23401153
165	Phosphorylation	MSSSGLGSPNRSSPS CCCCCCCCCCCCCCC	24.84	19664994
169	O-linked_Glycosylation	GLGSPNRSSPSIICM CCCCCCCCCCCEEEE	53.92	30059200
169	Phosphorylation	GLGSPNRSSPSIICM CCCCCCCCCCCEEEE	53.92	23401153
170	Phosphorylation	LGSPNRSSPSIICMP CCCCCCCCCCEEEEC	21.30	22167270
172	Phosphorylation	SPNRSSPSIICMPKQ CCCCCCCCEEEECCC	26.91	22167270
190	Phosphorylation	RQPFTVNSMSGFGMN CCCCEEECCCCCCCC	15.25	28555341
242	Phosphorylation	DRNRREGSGNPTPLI HCCCCCCCCCCCCCC	30.55	29255136
246	Phosphorylation	REGSGNPTPLINPLA CCCCCCCCCCCCCCC	34.42	25159151
258	Phosphorylation	PLAGRAPYVGMVTKP CCCCCCCEEEEEECC	14.51	24275569
270	Phosphorylation	TKPANEQSQDFSIHN ECCCCCCCCCCCCCC	26.07	23312004
274	Phosphorylation	NEQSQDFSIHNEDFP CCCCCCCCCCCCCCC	31.09	28555341
286	Phosphorylation	DFPALPGSSYKDPTS CCCCCCCCCCCCCCC	28.67	25627689
293	Phosphorylation	SSYKDPTSSNDDSKS CCCCCCCCCCCCCCC	32.31	-
294	Phosphorylation	SYKDPTSSNDDSKSN CCCCCCCCCCCCCCC	46.91	-
299	Acetylation	TSSNDDSKSNLNTSG CCCCCCCCCCCCCCC	50.81	7960613
304	Phosphorylation	DSKSNLNTSGKTTSS CCCCCCCCCCCCCCC	41.86	29214152
305	Phosphorylation	SKSNLNTSGKTTSST CCCCCCCCCCCCCCC	36.90	28985074
307	Ubiquitination	SNLNTSGKTTSSTDG CCCCCCCCCCCCCCC	48.69	-
308	Phosphorylation	NLNTSGKTTSSTDGP CCCCCCCCCCCCCCC	35.12	21712546
309	Phosphorylation	LNTSGKTTSSTDGPK CCCCCCCCCCCCCCC	24.94	28348404
310	Phosphorylation	NTSGKTTSSTDGPKF CCCCCCCCCCCCCCC	36.15	28348404
311	Phosphorylation	TSGKTTSSTDGPKFP CCCCCCCCCCCCCCC	28.55	28348404
312	Phosphorylation	SGKTTSSTDGPKFPG CCCCCCCCCCCCCCC	44.75	28348404
315 (in isoform 2)	Ubiquitination	-	37.61	21906983
321	Ubiquitination	GPKFPGDKSSTTQNN CCCCCCCCCCCCCCC	52.82	-
380	Phosphorylation	MVHLALGSDLTTLGL CEEEECCCCCEEECC	30.23	20068231
383	Phosphorylation	LALGSDLTTLGLNLN EECCCCCEEECCCCC	25.60	20068231
384	Phosphorylation	ALGSDLTTLGLNLNS ECCCCCEEECCCCCC	26.56	20068231
391	Phosphorylation	TLGLNLNSPENLYPK EECCCCCCHHHCCCC	36.44	29523821
396	Phosphorylation	LNSPENLYPKFASPW CCCHHHCCCCCCCCC	18.89	20090780
401	Phosphorylation	NLYPKFASPWASSPC HCCCCCCCCCCCCCC	24.90	28348404
405	Phosphorylation	KFASPWASSPCRPQD CCCCCCCCCCCCCCC	30.83	25159151
406	Phosphorylation	FASPWASSPCRPQDI CCCCCCCCCCCCCCC	21.92	25159151
440 (in isoform 5)	Ubiquitination	-	22.15	21906983
471	Phosphorylation	LFNRDWRYHKEERVW HHCCCCCCCCCCCEE	17.00	24719451
480	Phosphorylation	KEERVWITRAPGMEP CCCCEEEEECCCCCC	12.69	24719451
490	Ubiquitination	PGMEPTMKTNTYERG CCCCCCCCCCCEECC	40.89	2190698
490 (in isoform 1)	Ubiquitination	-	40.89	21906983
494	Phosphorylation	PTMKTNTYERGTYYF CCCCCCCEECCEEEE	13.00	30576142
499	Phosphorylation	NTYERGTYYFFDCLN CCEECCEEEEEEECC	10.91	30576142
500	Phosphorylation	TYERGTYYFFDCLNW CEECCEEEEEEECCH	9.52	-
512	Ubiquitination	LNWRKVAKEFHLEYD CCHHHHHHHHCCCHH	64.99	-
520	Ubiquitination	EFHLEYDKLEERPHL HHCCCHHHHHCCCCC	57.82	-

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
101	S	Phosphorylation	Kinase	ATR	Q13535	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CNOT2_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 CNOT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CNOT3_HUMAN	CNOT3	physical	16189514
NCOR2_HUMAN	NCOR2	physical	16712523
NCOR1_HUMAN	NCOR1	physical	16712523
GPS2_HUMAN	GPS2	physical	16712523
CNOT1_HUMAN	CNOT1	physical	16778766
CNOT3_HUMAN	CNOT3	physical	16778766
CNOT8_HUMAN	CNOT8	physical	16778766
CA2D1_HUMAN	CACNA2D1	physical	26496610
DDX11_HUMAN	DDX11	physical	26496610
FHL2_HUMAN	FHL2	physical	26496610
IF6_HUMAN	EIF6	physical	26496610
CNOT3_HUMAN	CNOT3	physical	26496610
DPOD1_HUMAN	POLD1	physical	26496610
RENT1_HUMAN	UPF1	physical	26496610
RL12_HUMAN	RPL12	physical	26496610
RT12_HUMAN	MRPS12	physical	26496610
XPO1_HUMAN	XPO1	physical	26496610
CNOT9_HUMAN	RQCD1	physical	26496610
CNOT8_HUMAN	CNOT8	physical	26496610
CNOT1_HUMAN	CNOT1	physical	26496610
UBP24_HUMAN	USP24	physical	26496610
LARP1_HUMAN	LARP1	physical	26496610
CNO10_HUMAN	CNOT10	physical	26496610
S18L2_HUMAN	SS18L2	physical	26496610
CNO11_HUMAN	CNOT11	physical	26496610
KANL3_HUMAN	KANSL3	physical	26496610
TM165_HUMAN	TMEM165	physical	26496610
AKIP1_HUMAN	AKIP1	physical	26496610
DDX24_HUMAN	DDX24	physical	26496610
WDR26_HUMAN	WDR26	physical	26496610
TB182_HUMAN	TNKS1BP1	physical	26496610
CNKR3_HUMAN	CNKSR3	physical	26496610
CNO6L_HUMAN	CNOT6L	physical	26496610
CNO11_HUMAN	CNOT11	physical	27173435
CNOT6_HUMAN	CNOT6	physical	27173435
CNOT7_HUMAN	CNOT7	physical	27173435
CNO10_HUMAN	CNOT10	physical	27173435
CNOT9_HUMAN	RQCD1	physical	27173435
CNOT1_HUMAN	CNOT1	physical	27173435

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 CNOT2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-165, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-165, 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 THR-93 AND SER-165, AND MASSSPECTROMETRY.	18669648 [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-165, AND MASSSPECTROMETRY.	18691976 [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-101, AND MASSSPECTROMETRY.	17525332 [Abstract]