dbPTM

CCNL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCNL2_HUMAN
UniProt AC	Q96S94
Protein Name	Cyclin-L2
Gene Name	CCNL2
Organism	Homo sapiens (Human).
Sequence Length	520
Subcellular Localization	Nucleus speckle . Nucleus, nucleoplasm .
Protein Description	Involved in pre-mRNA splicing. May induce cell death, possibly by acting on the transcription and RNA processing of apoptosis-related factors..
Protein Sequence	MAAAAAAAGAAGSAAPAAAAGAPGSGGAPSGSQGVLIGDRLYSGVLITLENCLLPDDKLRFTPSMSSGLDTDTETDLRVVGCELIQAAGILLRLPQVAMATGQVLFQRFFYTKSFVKHSMEHVSMACVHLASKIEEAPRRIRDVINVFHRLRQLRDKKKPVPLLLDQDYVNLKNQIIKAERRVLKELGFCVHVKHPHKIIVMYLQVLECERNQHLVQTSWNYMNDSLRTDVFVRFQPESIACACIYLAARTLEIPLPNRPHWFLLFGATEEEIQEICLKILQLYARKKVDLTHLEGEVEKRKHAIEEAKAQARGLLPGGTQVLDGTSGFSPAPKLVESPKEGKGSKPSPLSVKNTKRRLEGAKKAKADSPVNGLPKGRESRSRSRSREQSYSRSPSRSASPKRRKSDSGSTSGGSKSQSRSRSRSDSPPRQAPRSAPYKGSEIRGSRKSKDCKYPQKPHKSRSRSSSRSRSRSRERADNPGKYKKKSHYYRDQRRERSRSYERTGRRYERDHPGHSRHRR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAAAAG ------CHHHHHHHH	13.05	22223895
13	Phosphorylation	AAAGAAGSAAPAAAA HHHHHHHHHHHHHHC	19.28	28857561
25	Phosphorylation	AAAGAPGSGGAPSGS HHCCCCCCCCCCCCC	32.75	25159151
30	Phosphorylation	PGSGGAPSGSQGVLI CCCCCCCCCCCCEEE	51.01	25003641
32	Phosphorylation	SGGAPSGSQGVLIGD CCCCCCCCCCEEECC	28.26	28122231
42	Phosphorylation	VLIGDRLYSGVLITL EEECCEECCCCEEEE	12.31	27642862
101 (in isoform 2)	Phosphorylation	-	18.30	-
101	Phosphorylation	LPQVAMATGQVLFQR HHHHHHHHCCCHHHH	18.30	20068231
158	Ubiquitination	LRQLRDKKKPVPLLL HHHHHCCCCCCCEEE	67.60	29967540
159	Ubiquitination	RQLRDKKKPVPLLLD HHHHCCCCCCCEEEC	57.92	29967540
178	Ubiquitination	NLKNQIIKAERRVLK HHHHHHHHHHHHHHH	45.91	29967540
288	Ubiquitination	LQLYARKKVDLTHLE HHHHHCCCCCCCCCC	35.11	29967540
309	Ubiquitination	KHAIEEAKAQARGLL HHHHHHHHHHHCCCC	44.29	29967540
320	Phosphorylation	RGLLPGGTQVLDGTS CCCCCCCCEECCCCC	22.78	23403867
326	Phosphorylation	GTQVLDGTSGFSPAP CCEECCCCCCCCCCC	25.91	30266825
327	Phosphorylation	TQVLDGTSGFSPAPK CEECCCCCCCCCCCC	43.29	30266825
330	Phosphorylation	LDGTSGFSPAPKLVE CCCCCCCCCCCCCCC	24.55	29255136
338	Phosphorylation	PAPKLVESPKEGKGS CCCCCCCCCCCCCCC	33.52	28176443
345	Phosphorylation	SPKEGKGSKPSPLSV CCCCCCCCCCCCCCC	44.90	30266825
348	Phosphorylation	EGKGSKPSPLSVKNT CCCCCCCCCCCCHHH	42.06	22167270
351	Phosphorylation	GSKPSPLSVKNTKRR CCCCCCCCCHHHHHH	34.13	30266825
355	Phosphorylation	SPLSVKNTKRRLEGA CCCCCHHHHHHHHHH	21.88	23312004
364	Ubiquitination	RRLEGAKKAKADSPV HHHHHHHHHCCCCCC	55.36	-
366	Ubiquitination	LEGAKKAKADSPVNG HHHHHHHCCCCCCCC	62.70	-
369	Phosphorylation	AKKAKADSPVNGLPK HHHHCCCCCCCCCCC	35.29	19664994
390	Phosphorylation	RSRSREQSYSRSPSR HHHHCHHHHCCCCCC	21.96	25690035
391	Phosphorylation	SRSREQSYSRSPSRS HHHCHHHHCCCCCCC	14.06	25690035
394	Phosphorylation	REQSYSRSPSRSASP CHHHHCCCCCCCCCC	22.68	24247654
400	Phosphorylation	RSPSRSASPKRRKSD CCCCCCCCCCCCCCC	32.00	-
406	Phosphorylation	ASPKRRKSDSGSTSG CCCCCCCCCCCCCCC	34.89	20068231
408	Phosphorylation	PKRRKSDSGSTSGGS CCCCCCCCCCCCCCC	41.56	20068231
410	Phosphorylation	RRKSDSGSTSGGSKS CCCCCCCCCCCCCHH	24.29	20068231
411	Phosphorylation	RKSDSGSTSGGSKSQ CCCCCCCCCCCCHHC	34.61	20068231
412	Phosphorylation	KSDSGSTSGGSKSQS CCCCCCCCCCCHHCC	42.74	20068231
415	Phosphorylation	SGSTSGGSKSQSRSR CCCCCCCCHHCCCCC	32.43	20068231
417	Phosphorylation	STSGGSKSQSRSRSR CCCCCCHHCCCCCCC	34.78	20068231
419	Phosphorylation	SGGSKSQSRSRSRSD CCCCHHCCCCCCCCC	39.04	20068231
423	Phosphorylation	KSQSRSRSRSDSPPR HHCCCCCCCCCCCCC	37.07	21406692
425	Phosphorylation	QSRSRSRSDSPPRQA CCCCCCCCCCCCCCC	43.62	21406692
427	Phosphorylation	RSRSRSDSPPRQAPR CCCCCCCCCCCCCCC	37.74	21406692
435	Phosphorylation	PPRQAPRSAPYKGSE CCCCCCCCCCCCCCC	32.32	25159151
441	Phosphorylation	RSAPYKGSEIRGSRK CCCCCCCCCCCCCCC	26.21	25159151
449	O-linked_Glycosylation	EIRGSRKSKDCKYPQ CCCCCCCCCCCCCCC	32.39	30379171
461	Phosphorylation	YPQKPHKSRSRSSSR CCCCCCCCCCCCCCH	32.24	24719451
463	Phosphorylation	QKPHKSRSRSSSRSR CCCCCCCCCCCCHHH	43.54	20068231
465	Phosphorylation	PHKSRSRSSSRSRSR CCCCCCCCCCHHHHH	33.63	24260401
466	Phosphorylation	HKSRSRSSSRSRSRS CCCCCCCCCHHHHHH	28.76	22210691
467	Phosphorylation	KSRSRSSSRSRSRSR CCCCCCCCHHHHHHH	35.21	22210691
471	Phosphorylation	RSSSRSRSRSRERAD CCCCHHHHHHHHCCC	35.54	20068231
473	Phosphorylation	SSRSRSRSRERADNP CCHHHHHHHHCCCCC	39.48	20068231
482	Acetylation	ERADNPGKYKKKSHY HCCCCCCCCCCCHHH	55.97	7704487
483	Phosphorylation	RADNPGKYKKKSHYY CCCCCCCCCCCHHHH	33.67	-
498	Phosphorylation	RDQRRERSRSYERTG HHHHHHHHHHHHHHC	22.33	20068231
500	Phosphorylation	QRRERSRSYERTGRR HHHHHHHHHHHHCCC	32.37	20068231
501	Phosphorylation	RRERSRSYERTGRRY HHHHHHHHHHHCCCC	14.34	21406692
516	Phosphorylation	ERDHPGHSRHRR--- CCCCCCCCCCCC---	35.38	-

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
330	S	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
338	S	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
369	S	Phosphorylation	Kinase	DYRK1A	Q13627	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CCNL2_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 CCNL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPB1_HUMAN	POLR2A	physical	14684736
ASM3B_HUMAN	SMPDL3B	physical	26186194
GNAZ_HUMAN	GNAZ	physical	26186194
GNA11_HUMAN	GNA11	physical	26186194
GNAQ_HUMAN	GNAQ	physical	26186194
PTPRG_HUMAN	PTPRG	physical	26186194
AP1B1_HUMAN	AP1B1	physical	26186194
FYN_HUMAN	FYN	physical	26186194
YES_HUMAN	YES1	physical	26186194
LYN_HUMAN	LYN	physical	26186194
SRC_HUMAN	SRC	physical	26186194
ABCF2_HUMAN	ABCF2	physical	26186194
PYGB_HUMAN	PYGB	physical	26186194
I2BP2_HUMAN	IRF2BP2	physical	26186194
ULBP3_HUMAN	ULBP3	physical	26186194
SNX1_HUMAN	SNX1	physical	26186194
IREB2_HUMAN	IREB2	physical	26186194
DIAP1_HUMAN	DIAPH1	physical	26186194
EHD1_HUMAN	EHD1	physical	26186194
CNTN1_HUMAN	CNTN1	physical	26186194
MERL_HUMAN	NF2	physical	26186194
GBB4_HUMAN	GNB4	physical	26186194
NEUM_HUMAN	GAP43	physical	26186194
CSTF3_HUMAN	CSTF3	physical	26186194
KPCA_HUMAN	PRKCA	physical	26186194
RRAS_HUMAN	RRAS	physical	26186194
SNX6_HUMAN	SNX6	physical	26186194
KAPCB_HUMAN	PRKACB	physical	26186194
I2BP1_HUMAN	IRF2BP1	physical	26186194
CCNY_HUMAN	CCNY	physical	26186194
NSDHL_HUMAN	NSDHL	physical	26186194
EPCR_HUMAN	PROCR	physical	26186194
DCAF1_HUMAN	VPRBP	physical	25532805
SAMH1_HUMAN	SAMHD1	physical	25532805
CCNY_HUMAN	CCNY	physical	28514442
SRC_HUMAN	SRC	physical	28514442
I2BP1_HUMAN	IRF2BP1	physical	28514442
IREB2_HUMAN	IREB2	physical	28514442
MERL_HUMAN	NF2	physical	28514442
OCC1_HUMAN	C12orf75	physical	28514442
ZBT43_HUMAN	ZBTB43	physical	28514442
PTPRG_HUMAN	PTPRG	physical	28514442
ULBP3_HUMAN	ULBP3	physical	28514442
CNTN1_HUMAN	CNTN1	physical	28514442
RRAS_HUMAN	RRAS	physical	28514442
CSTF3_HUMAN	CSTF3	physical	28514442
YES_HUMAN	YES1	physical	28514442
FYN_HUMAN	FYN	physical	28514442
NEUM_HUMAN	GAP43	physical	28514442
GNAZ_HUMAN	GNAZ	physical	28514442
GNAQ_HUMAN	GNAQ	physical	28514442
I2BP2_HUMAN	IRF2BP2	physical	28514442
SNX1_HUMAN	SNX1	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 CCNL2_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-330 AND SER-369, AND MASS SPECTROMETRY.	19413330 [Abstract]
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-330 AND SER-369, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-330 AND SER-369, AND MASS SPECTROMETRY.	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-369, AND MASSSPECTROMETRY.	18669648 [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-345; SER-351 ANDSER-369, AND MASS SPECTROMETRY.	17081983 [Abstract]