dbPTM

CDCA7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDCA7_HUMAN
UniProt AC	Q9BWT1
Protein Name	Cell division cycle-associated protein 7
Gene Name	CDCA7
Organism	Homo sapiens (Human).
Sequence Length	371
Subcellular Localization	Nucleus. Cytoplasm. Predominantly nuclear with some expression also seen in the cytoplasm. Predominantly cytoplasmic when phosphorylated at Thr-163.
Protein Description	Participates in MYC-mediated cell transformation and apoptosis; induces anchorage-independent growth and clonogenicity in lymphoblastoid cells. Insufficient to induce tumorigenicity when overexpressed but contributes to MYC-mediated tumorigenesis. May play a role as transcriptional regulator..
Protein Sequence	MDARRVPQKDLRVKKNLKKFRYVKLISMETSSSSDDSCDSFASDNFANTRLQSVREGCRTRSQCRHSGPLRVAMKFPARSTRGATNKKAESRQPSENSVTDSNSDSEDESGMNFLEKRALNIKQNKAMLAKLMSELESFPGSFRGRHPLPGSDSQSRRPRRRTFPGVASRRNPERRARPLTRSRSRILGSLDALPMEEEEEEDKYMLVRKRKTVDGYMNEDDLPRSRRSRSSVTLPHIIRPVEEITEEELENVCSNSREKIYNRSLGSTCHQCRQKTIDTKTNCRNPDCWGVRGQFCGPCLRNRYGEEVRDALLDPNWHCPPCRGICNCSFCRQRDGRCATGVLVYLAKYHGFGNVHAYLKSLKQEFEMQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Ubiquitination	DARRVPQKDLRVKKN CCCCCCHHHHHHHHH	53.30	-
9	Acetylation	DARRVPQKDLRVKKN CCCCCCHHHHHHHHH	53.30	23749302
9 (in isoform 2)	Ubiquitination	-	53.30	-
9	Ubiquitination	DARRVPQKDLRVKKN CCCCCCHHHHHHHHH	53.30	-
9	Acetylation	DARRVPQKDLRVKKN CCCCCCHHHHHHHHH	53.30	-
27 (in isoform 2)	Phosphorylation	-	22.47	24144214
30 (in isoform 2)	Phosphorylation	-	25.85	24144214
31	Phosphorylation	KLISMETSSSSDDSC EEEEEECCCCCCCCC	18.21	28634120
31 (in isoform 2)	Phosphorylation	-	18.21	24144214
32 (in isoform 2)	Phosphorylation	-	41.08	24144214
33	Ubiquitination	ISMETSSSSDDSCDS EEEECCCCCCCCCHH	37.24	-
33 (in isoform 2)	Phosphorylation	-	37.24	24144214
34 (in isoform 2)	Phosphorylation	-	47.59	24144214
37 (in isoform 2)	Phosphorylation	-	25.47	24144214
43 (in isoform 2)	Phosphorylation	-	30.95	24144214
67	Phosphorylation	TRSQCRHSGPLRVAM CHHHCCCCCCEEEEE	23.82	24719451
75	Ubiquitination	GPLRVAMKFPARSTR CCEEEEEECCCCCCC	38.16	-
75	Sumoylation	GPLRVAMKFPARSTR CCEEEEEECCCCCCC	38.16	-
75	Sumoylation	GPLRVAMKFPARSTR CCEEEEEECCCCCCC	38.16	-
75	Acetylation	GPLRVAMKFPARSTR CCEEEEEECCCCCCC	38.16	25953088
80	Phosphorylation	AMKFPARSTRGATNK EEECCCCCCCCCCCC	25.27	-
81	Phosphorylation	MKFPARSTRGATNKK EECCCCCCCCCCCCC	27.80	-
81	Ubiquitination	MKFPARSTRGATNKK EECCCCCCCCCCCCC	27.80	-
84	Ubiquitination	PARSTRGATNKKAES CCCCCCCCCCCCCCC	12.52	-
89	Ubiquitination	RGATNKKAESRQPSE CCCCCCCCCCCCCCC	22.93	-
91	Phosphorylation	ATNKKAESRQPSENS CCCCCCCCCCCCCCC	40.87	21406692
95	Phosphorylation	KAESRQPSENSVTDS CCCCCCCCCCCCCCC	40.86	28450419
98	Phosphorylation	SRQPSENSVTDSNSD CCCCCCCCCCCCCCC	23.49	28450419
100	Phosphorylation	QPSENSVTDSNSDSE CCCCCCCCCCCCCCC	33.27	28450419
102	Phosphorylation	SENSVTDSNSDSEDE CCCCCCCCCCCCCCH	28.94	28450419
104	Phosphorylation	NSVTDSNSDSEDESG CCCCCCCCCCCCHHH	46.60	28450419
106	Phosphorylation	VTDSNSDSEDESGMN CCCCCCCCCCHHHHH	46.93	28450419
110	Phosphorylation	NSDSEDESGMNFLEK CCCCCCHHHHHHHHH	56.52	28450419
117	Acetylation	SGMNFLEKRALNIKQ HHHHHHHHHHHCHHH	45.15	26051181
123	Ubiquitination	EKRALNIKQNKAMLA HHHHHCHHHHHHHHH	46.90	22505724
123	Acetylation	EKRALNIKQNKAMLA HHHHHCHHHHHHHHH	46.90	25953088
126	Ubiquitination	ALNIKQNKAMLAKLM HHCHHHHHHHHHHHH	32.45	29967540
131	Ubiquitination	QNKAMLAKLMSELES HHHHHHHHHHHHHHC	40.54	-
131	Sumoylation	QNKAMLAKLMSELES HHHHHHHHHHHHHHC	40.54	-
131	Sumoylation	QNKAMLAKLMSELES HHHHHHHHHHHHHHC	40.54	-
138	Phosphorylation	KLMSELESFPGSFRG HHHHHHHCCCCCCCC	49.74	26074081
142	Phosphorylation	ELESFPGSFRGRHPL HHHCCCCCCCCCCCC	16.41	26074081
146 (in isoform 2)	Phosphorylation	-	24.80	24719451
152	Phosphorylation	GRHPLPGSDSQSRRP CCCCCCCCCCCCCCC	31.95	28555341
154	Phosphorylation	HPLPGSDSQSRRPRR CCCCCCCCCCCCCCC	31.58	28555341
154 (in isoform 2)	Ubiquitination	-	31.58	-
162	Ubiquitination	QSRRPRRRTFPGVAS CCCCCCCCCCCCHHH	41.83	-
163	Phosphorylation	SRRPRRRTFPGVASR CCCCCCCCCCCHHHC	32.16	30576142
168	Ubiquitination	RRTFPGVASRRNPER CCCCCCHHHCCCHHH	11.84	-
170	Ubiquitination	TFPGVASRRNPERRA CCCCHHHCCCHHHHC	32.43	-
174 (in isoform 2)	Phosphorylation	-	59.35	21406692
175	Ubiquitination	ASRRNPERRARPLTR HHCCCHHHHCCCCCH	38.52	22505724
177 (in isoform 2)	Phosphorylation	-	24.54	21406692
179 (in isoform 2)	Phosphorylation	-	36.78	21406692
181 (in isoform 2)	Phosphorylation	-	29.31	21406692
183 (in isoform 2)	Phosphorylation	-	29.40	21406692
185 (in isoform 2)	Phosphorylation	-	25.56	21406692
190	Phosphorylation	SRSRILGSLDALPME HHHHHHHCCCCCCCC	21.45	28674151
202 (in isoform 2)	Ubiquitination	-	64.18	-
202	Ubiquitination	PMEEEEEEDKYMLVR CCCCHHHHHCEEEEE	64.18	22505724
204	Sumoylation	EEEEEEDKYMLVRKR CCHHHHHCEEEEECC	35.52	28112733
204	Ubiquitination	EEEEEEDKYMLVRKR CCHHHHHCEEEEECC	35.52	-
205	Ubiquitination	EEEEEDKYMLVRKRK CHHHHHCEEEEECCC	14.17	29967540
205 (in isoform 2)	Ubiquitination	-	14.17	-
205	Phosphorylation	EEEEEDKYMLVRKRK CHHHHHCEEEEECCC	14.17	28796482
210	Ubiquitination	DKYMLVRKRKTVDGY HCEEEEECCCCCCCC	51.25	22505724
210 (in isoform 2)	Ubiquitination	-	51.25	-
212	Ubiquitination	YMLVRKRKTVDGYMN EEEEECCCCCCCCCC	56.80	22505724
213	Phosphorylation	MLVRKRKTVDGYMNE EEEECCCCCCCCCCH	28.06	28555341
229	Phosphorylation	DLPRSRRSRSSVTLP HCCCCHHCCCCCCHH	35.09	25627689
231	Phosphorylation	PRSRRSRSSVTLPHI CCCHHCCCCCCHHHE	30.33	25627689
242	Phosphorylation	LPHIIRPVEEITEEE HHHEECCHHHCCHHH	8.07	32645325
262	Ubiquitination	SNSREKIYNRSLGST CCCHHHHHHCHHCHH	18.65	22505724
264	Ubiquitination	SREKIYNRSLGSTCH CHHHHHHCHHCHHHH	19.11	22505724
269 (in isoform 2)	Phosphorylation	-	16.53	24719451
276	Ubiquitination	TCHQCRQKTIDTKTN HHHHHHHHCCCCCCC	28.26	29967540
280 (in isoform 3)	Phosphorylation	-	35.60	30631047
283 (in isoform 2)	Ubiquitination	-	25.06	-
284 (in isoform 2)	Phosphorylation	-	5.57	27642862
289	Ubiquitination	TNCRNPDCWGVRGQF CCCCCCCCCCCCCCC	3.43	22505724
289 (in isoform 2)	Ubiquitination	-	3.43	-
291	Ubiquitination	CRNPDCWGVRGQFCG CCCCCCCCCCCCCCH	12.94	22505724
291 (in isoform 2)	Ubiquitination	-	12.94	-
307	Ubiquitination	CLRNRYGEEVRDALL HHHHCCCHHHHHHHH	44.37	-
319	Ubiquitination	ALLDPNWHCPPCRGI HHHCCCCCCCCCCCE	22.35	-
322	Ubiquitination	DPNWHCPPCRGICNC CCCCCCCCCCCEECC	26.32	-
349	Ubiquitination	GVLVYLAKYHGFGNV HHHHHHHHHCCCCCH	34.87	-
350	Phosphorylation	VLVYLAKYHGFGNVH HHHHHHHHCCCCCHH	11.10	24114839
355	Ubiquitination	AKYHGFGNVHAYLKS HHHCCCCCHHHHHHH	21.82	29967540
359	Phosphorylation	GFGNVHAYLKSLKQE CCCCHHHHHHHHHHH	10.37	24114839
361	Ubiquitination	GNVHAYLKSLKQEFE CCHHHHHHHHHHHHH	40.86	29967540
364	Sumoylation	HAYLKSLKQEFEMQA HHHHHHHHHHHHHCC	55.67	-
364	Ubiquitination	HAYLKSLKQEFEMQA HHHHHHHHHHHHHCC	55.67	22505724
364	Sumoylation	HAYLKSLKQEFEMQA HHHHHHHHHHHHHCC	55.67	-
416	Ubiquitination	---------------------------------------------------- ----------------------------------------------------		22505724
428 (in isoform 2)	Ubiquitination	-		-
440	Ubiquitination	---------------------------------------------------------------------------- ----------------------------------------------------------------------------		29967540
440 (in isoform 2)	Ubiquitination	-		-
443 (in isoform 2)	Ubiquitination	-		-
443	Ubiquitination	------------------------------------------------------------------------------- -------------------------------------------------------------------------------		22505724

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
163	T	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
163	T	Phosphorylation	23186163
In vitro, phosphorylated at Thr-163 by AKT.
163	T	Phosphorylation	23186163
Phosphorylation at Thr-163 promotes interaction with YWHAE and YWHAZ, dissociation from MYC and sequestration in the cytoplasm.

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 CDCA7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
1433T_HUMAN	YWHAQ	physical	26186194
1433S_HUMAN	SFN	physical	26186194
1433Z_HUMAN	YWHAZ	physical	26186194
1433F_HUMAN	YWHAH	physical	26186194
1433Z_HUMAN	YWHAZ	physical	28514442
1433G_HUMAN	YWHAG	physical	28514442
1433F_HUMAN	YWHAH	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 CDCA7_HUMAN

Related Literatures of Post-Translational Modification

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