dbPTM

CDCA5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDCA5_HUMAN
UniProt AC	Q96FF9
Protein Name	Sororin
Gene Name	CDCA5
Organism	Homo sapiens (Human).
Sequence Length	252
Subcellular Localization	Nucleus . Chromosome . Cytoplasm . Associates with nuclear chromatin from S phase until metaphase and is released in the cytoplasm upon nuclear envelope breakdown.
Protein Description	Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair..
Protein Sequence	MSGRRTRSGGAAQRSGPRAPSPTKPLRRSQRKSGSELPSILPEIWPKTPSAAAVRKPIVLKRIVAHAVEVPAVQSPRRSPRISFFLEKENEPPGRELTKEDLFKTHSVPATPTSTPVPNPEAESSSKEGELDARDLEMSKKVRRSYSRLETLGSASTSTPGRRSCFGFEGLLGAEDLSGVSPVVCSKLTEVPRVCAKPWAPDMTLPGISPPPEKQKRKKKKMPEILKTELDEWAAAMNAEFEAAEQFDLLVE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MSGRRTRSGGAAQ --CCCCCCCCCCCCC	28.03	29759185
15	Phosphorylation	SGGAAQRSGPRAPSP CCCCCCCCCCCCCCC	40.86	20363803
21	Phosphorylation	RSGPRAPSPTKPLRR CCCCCCCCCCCCCCH	44.19	29255136
23	Phosphorylation	GPRAPSPTKPLRRSQ CCCCCCCCCCCCHHH	50.02	22167270
29	Phosphorylation	PTKPLRRSQRKSGSE CCCCCCHHHCCCCCC	28.09	18669648
33	Phosphorylation	LRRSQRKSGSELPSI CCHHHCCCCCCCCCC	50.14	25159151
35	Phosphorylation	RSQRKSGSELPSILP HHHCCCCCCCCCCCC	42.95	25159151
39	Phosphorylation	KSGSELPSILPEIWP CCCCCCCCCCCHHCC	49.75	20873877
48	Phosphorylation	LPEIWPKTPSAAAVR CCHHCCCCCCHHHHC	20.56	25159151
50	Phosphorylation	EIWPKTPSAAAVRKP HHCCCCCCHHHHCCC	35.45	25159151
61	Methylation	VRKPIVLKRIVAHAV HCCCHHHHHHHHHHH	29.23	-
75	Phosphorylation	VEVPAVQSPRRSPRI HCCCCCCCCCCCCCE	17.49	29255136
79	Phosphorylation	AVQSPRRSPRISFFL CCCCCCCCCCEEEEE	21.58	25159151
83	Phosphorylation	PRRSPRISFFLEKEN CCCCCCEEEEEECCC	15.95	25463755
98	Phosphorylation	EPPGRELTKEDLFKT CCCCCCCCHHHHHHH	27.86	23186163
99	Ubiquitination	PPGRELTKEDLFKTH CCCCCCCHHHHHHHC	62.95	21890473
104	Ubiquitination	LTKEDLFKTHSVPAT CCHHHHHHHCCCCCC	53.26	-
105	Phosphorylation	TKEDLFKTHSVPATP CHHHHHHHCCCCCCC	16.43	26055452
107	Phosphorylation	EDLFKTHSVPATPTS HHHHHHCCCCCCCCC	34.72	25159151
111	Phosphorylation	KTHSVPATPTSTPVP HHCCCCCCCCCCCCC	22.49	25159151
113	Phosphorylation	HSVPATPTSTPVPNP CCCCCCCCCCCCCCC	40.66	25159151
114	Phosphorylation	SVPATPTSTPVPNPE CCCCCCCCCCCCCCC	31.73	25159151
115	Phosphorylation	VPATPTSTPVPNPEA CCCCCCCCCCCCCCH	30.68	25159151
124	Phosphorylation	VPNPEAESSSKEGEL CCCCCHHCCCCCCCC	47.13	25159151
125	Phosphorylation	PNPEAESSSKEGELD CCCCHHCCCCCCCCC	36.61	25159151
126	Phosphorylation	NPEAESSSKEGELDA CCCHHCCCCCCCCCH	43.96	25159151
139	Phosphorylation	DARDLEMSKKVRRSY CHHHHHHHHHHHHHH	21.68	-
145	Phosphorylation	MSKKVRRSYSRLETL HHHHHHHHHHHHHHH	19.52	25159151
146	Phosphorylation	SKKVRRSYSRLETLG HHHHHHHHHHHHHHC	8.94	29214152
147	Phosphorylation	KKVRRSYSRLETLGS HHHHHHHHHHHHHCC	31.47	22617229
151	Phosphorylation	RSYSRLETLGSASTS HHHHHHHHHCCCCCC	40.80	21712546
154	Phosphorylation	SRLETLGSASTSTPG HHHHHHCCCCCCCCC	23.35	25159151
156	Phosphorylation	LETLGSASTSTPGRR HHHHCCCCCCCCCCH	25.29	30266825
157	Phosphorylation	ETLGSASTSTPGRRS HHHCCCCCCCCCCHH	36.01	30266825
158	Phosphorylation	TLGSASTSTPGRRSC HHCCCCCCCCCCHHH	30.06	30266825
159	Phosphorylation	LGSASTSTPGRRSCF HCCCCCCCCCCHHHC	29.83	30266825
164	Phosphorylation	TSTPGRRSCFGFEGL CCCCCCHHHCCCCCC	16.67	22777824
178	Phosphorylation	LLGAEDLSGVSPVVC CCCCHHCCCCCCCCC	49.85	20068231
181	Phosphorylation	AEDLSGVSPVVCSKL CHHCCCCCCCCCCCC	18.59	25159151
186	Phosphorylation	GVSPVVCSKLTEVPR CCCCCCCCCCCCCCC	21.06	20068231
197	Acetylation	EVPRVCAKPWAPDMT CCCCCCCCCCCCCCC	35.65	26051181
197	Ubiquitination	EVPRVCAKPWAPDMT CCCCCCCCCCCCCCC	35.65	-
204	Phosphorylation	KPWAPDMTLPGISPP CCCCCCCCCCCCCCC	36.86	27050516
209	Phosphorylation	DMTLPGISPPPEKQK CCCCCCCCCCHHHHH	36.95	28731282

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
21	S	Phosphorylation	Kinase	CDK1	P06493	PSP
33	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
33	S	Phosphorylation	Kinase	CDK1	P06493	PSP
48	T	Phosphorylation	Kinase	CDK1	P06493	PSP
75	S	Phosphorylation	Kinase	CDK1	P06493	PSP
79	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
79	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
79	S	Phosphorylation	Kinase	CDK1	P06493	PSP
79	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
83	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
83	S	Phosphorylation	Kinase	CDK1	P06493	PSP
111	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
111	T	Phosphorylation	Kinase	CDK1	P06493	PSP
115	T	Phosphorylation	Kinase	PLK1	P53350	PSP
115	T	Phosphorylation	Kinase	CDK1	P06493	PSP
115	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
126	S	Phosphorylation	Kinase	CDK1	P06493	PSP
126	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
139	S	Phosphorylation	Kinase	CDK1	P06493	PSP
139	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
151	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
151	T	Phosphorylation	Kinase	CDK1	P06493	PSP
151	T	Phosphorylation	Kinase	PLK1	P53350	PSP
159	T	Phosphorylation	Kinase	CDK1	P06493	PSP
159	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
164	S	Phosphorylation	Kinase	CDK1	P06493	PSP
164	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
181	S	Phosphorylation	Kinase	CDK1	P06493	PSP
209	S	Phosphorylation	Kinase	CDK1	P06493	PSP
209	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
209	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CDCA5_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 CDCA5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC6_HUMAN	XRCC6	physical	16169070
SMC3_HUMAN	SMC3	physical	15837422
PDS5A_HUMAN	PDS5A	physical	15837422
PDS5B_HUMAN	PDS5B	physical	15837422
RAD21_HUMAN	RAD21	physical	15837422
CDCA5_HUMAN	CDCA5	physical	20360068
NAA16_HUMAN	NAA16	physical	22939629
LARP1_HUMAN	LARP1	physical	22939629
CETN2_HUMAN	CETN2	physical	22939629
PDS5B_HUMAN	PDS5B	physical	21111234
PDS5A_HUMAN	PDS5A	physical	21111234
RAD21_HUMAN	RAD21	physical	21111234
SMC3_HUMAN	SMC3	physical	21111234
PLK1_HUMAN	PLK1	physical	21987589
STAG2_HUMAN	STAG2	physical	21987589
RAD21_HUMAN	RAD21	physical	21987589
TTLL3_HUMAN	TTLL3	physical	21988832
IRAK3_HUMAN	IRAK3	physical	21988832
SENP2_HUMAN	SENP2	physical	21988832
RIP_HUMAN	RPAIN	physical	21988832
KDM1A_HUMAN	KDM1A	physical	23455924
SMC1A_HUMAN	SMC1A	physical	26186194
SMC3_HUMAN	SMC3	physical	26186194
ZY11B_HUMAN	ZYG11B	physical	26186194
STAG2_HUMAN	STAG2	physical	26186194
NAA10_HUMAN	NAA10	physical	26186194
RAD21_HUMAN	RAD21	physical	26186194
SMC1B_HUMAN	SMC1B	physical	26186194
ZER1_HUMAN	ZER1	physical	26186194
MGME1_HUMAN	MGME1	physical	26186194
BTD_HUMAN	BTD	physical	26496610
CENPF_HUMAN	CENPF	physical	26496610
H33_HUMAN	H3F3A	physical	26496610
HSP7C_HUMAN	HSPA8	physical	26496610
E2AK2_HUMAN	EIF2AK2	physical	26496610
RAD21_HUMAN	RAD21	physical	26496610
RBM4_HUMAN	RBM4	physical	26496610
TBX3_HUMAN	TBX3	physical	26496610
VINC_HUMAN	VCL	physical	26496610
BAG6_HUMAN	BAG6	physical	26496610
SMC1A_HUMAN	SMC1A	physical	26496610
MBD2_HUMAN	MBD2	physical	26496610
SMC3_HUMAN	SMC3	physical	26496610
NHRF1_HUMAN	SLC9A3R1	physical	26496610
DNM1L_HUMAN	DNM1L	physical	26496610
GEPH_HUMAN	GPHN	physical	26496610
STAG1_HUMAN	STAG1	physical	26496610
STAG2_HUMAN	STAG2	physical	26496610
CDC37_HUMAN	CDC37	physical	26496610
PDS5B_HUMAN	PDS5B	physical	26496610
WAPL_HUMAN	WAPAL	physical	26496610
PDS5A_HUMAN	PDS5A	physical	26496610
BDP1_HUMAN	BDP1	physical	26496610
BHE41_HUMAN	BHLHE41	physical	26496610
DOCK5_HUMAN	DOCK5	physical	26496610
FIP1_HUMAN	FIP1L1	physical	26496610
C99L2_HUMAN	CD99L2	physical	26496610
OBSCN_HUMAN	OBSCN	physical	26496610
CHD6_HUMAN	CHD6	physical	26496610
ERI1_HUMAN	ERI1	physical	26496610
TCAM1_HUMAN	TICAM1	physical	26496610
SCAI_HUMAN	SCAI	physical	26496610
SMC1A_HUMAN	SMC1A	genetic	26895426
RAD21_HUMAN	RAD21	physical	28514442
STAG2_HUMAN	STAG2	physical	28514442
ZY11B_HUMAN	ZYG11B	physical	28514442
SMC3_HUMAN	SMC3	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 CDCA5_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-75; THR-105; SER-107 ANDTHR-115, AND MASS 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-35 AND SER-209, 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-29; SER-33; SER-35;SER-75; SER-79; SER-83; THR-105; THR-111; THR-115 AND SER-209, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND THR-159, AND MASSSPECTROMETRY.	18220336 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48 AND SER-50, AND MASSSPECTROMETRY.	16964243 [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-75 AND SER-79, AND MASSSPECTROMETRY.	17081983 [Abstract]