dbPTM

CDC16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CDC16_HUMAN
UniProt AC	Q13042
Protein Name	Cell division cycle protein 16 homolog
Gene Name	CDC16
Organism	Homo sapiens (Human).
Sequence Length	620
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Colocalizes with CDC27 to the centrosome at all stages of the cell cycle and to the mitotic spindle.
Protein Description	Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains..
Protein Sequence	MNLERLRKRVRQYLDQQQYQSALFWADKVASLSREEPQDIYWLAQCLYLTAQYHRAAHALRSRKLDKLYEACRYLAARCHYAAKEHQQALDVLDMEEPINKRLFEKYLKDESGFKDPSSDWEMSQSSIKSSICLLRGKIYDALDNRTLATYSYKEALKLDVYCFEAFDLLTSHHMLTAQEEKELLESLPLSKLCNEEQELLRFLFENKLKKYNKPSETVIPESVDGLQENLDVVVSLAERHYYNCDFKMCYKLTSVVMEKDPFHASCLPVHIGTLVELNKANELFYLSHKLVDLYPSNPVSWFAVGCYYLMVGHKNEHARRYLSKATTLEKTYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAERFFSQALSIAPEDPFVMHEVGVVAFQNGEWKTAEKWFLDALEKIKAIGNEVTVDKWEPLLNNLGHVCRKLKKYAEALDYHRQALVLIPQNASTYSAIGYIHSLMGNFENAVDYFHTALGLRRDDTFSVTMLGHCIEMYIGDSEAYIGADIKDKLKCYDFDVHTMKTLKNIISPPWDFREFEVEKQTAEETGLTPLETSRKTPDSRPSLEETFEIEMNESDMMLETSMSDHST

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Ubiquitination	RLRKRVRQYLDQQQY HHHHHHHHHHHHHHH	40.04	21890473
21	Ubiquitination	LDQQQYQSALFWADK HHHHHHHHHHHHHHH	23.23	21890473
28	Ubiquitination	SALFWADKVASLSRE HHHHHHHHHHHCCCC	31.77	-
31	Phosphorylation	FWADKVASLSREEPQ HHHHHHHHCCCCCCH	29.84	27174698
33	Phosphorylation	ADKVASLSREEPQDI HHHHHHCCCCCCHHH	34.84	27174698
41	Phosphorylation	REEPQDIYWLAQCLY CCCCHHHHHHHHHHH	11.58	29978859
48	Phosphorylation	YWLAQCLYLTAQYHR HHHHHHHHHHHHHHH	15.05	29978859
50	Phosphorylation	LAQCLYLTAQYHRAA HHHHHHHHHHHHHHH	9.73	29978859
53	Phosphorylation	CLYLTAQYHRAAHAL HHHHHHHHHHHHHHH	7.27	29978859
60	Ubiquitination	YHRAAHALRSRKLDK HHHHHHHHHHCHHHH	3.52	21890473
101	Acetylation	DMEEPINKRLFEKYL CCCCCHHHHHHHHHH	51.72	26051181
101	Ubiquitination	DMEEPINKRLFEKYL CCCCCHHHHHHHHHH	51.72	-
105 (in isoform 2)	Ubiquitination	-	45.44	21890473
105 (in isoform 3)	Ubiquitination	-	45.44	21890473
106	Ubiquitination	INKRLFEKYLKDESG HHHHHHHHHHCCCCC	48.85	21890473
106 (in isoform 1)	Ubiquitination	-	48.85	21890473
109	Ubiquitination	RLFEKYLKDESGFKD HHHHHHHCCCCCCCC	57.25	-
109	Acetylation	RLFEKYLKDESGFKD HHHHHHHCCCCCCCC	57.25	26051181
112	Phosphorylation	EKYLKDESGFKDPSS HHHHCCCCCCCCCCC	60.71	22199227
114 (in isoform 2)	Ubiquitination	-	12.96	21890473
114 (in isoform 3)	Ubiquitination	-	12.96	21890473
115	Ubiquitination	LKDESGFKDPSSDWE HCCCCCCCCCCCCCC	72.72	21906983
115 (in isoform 1)	Ubiquitination	-	72.72	21890473
118	Phosphorylation	ESGFKDPSSDWEMSQ CCCCCCCCCCCCCCH	51.57	29083192
119	Phosphorylation	SGFKDPSSDWEMSQS CCCCCCCCCCCCCHH	52.73	29083192
124	Phosphorylation	PSSDWEMSQSSIKSS CCCCCCCCHHHHHHH	18.52	29083192
126	Phosphorylation	SDWEMSQSSIKSSIC CCCCCCHHHHHHHHH	27.07	29083192
129	Ubiquitination	EMSQSSIKSSICLLR CCCHHHHHHHHHHHH	39.85	-
138	Ubiquitination	SICLLRGKIYDALDN HHHHHHCCHHHHCCC	31.49	-
140	Phosphorylation	CLLRGKIYDALDNRT HHHHCCHHHHCCCCE	9.92	29496907
153 (in isoform 3)	Ubiquitination	-	11.48	21890473
153 (in isoform 2)	Ubiquitination	-	11.48	21890473
154 (in isoform 1)	Ubiquitination	-	30.48	21890473
154	Ubiquitination	TLATYSYKEALKLDV EEEEECHHHHHCCCE	30.48	21890473
192	Ubiquitination	LESLPLSKLCNEEQE HHHCCHHHHCCHHHH	65.82	-
208	Ubiquitination	LRFLFENKLKKYNKP HHHHHHHHHHHCCCC	55.26	-
212	Phosphorylation	FENKLKKYNKPSETV HHHHHHHCCCCCCCC	27.17	29759185
216	Phosphorylation	LKKYNKPSETVIPES HHHCCCCCCCCCCCC	47.73	29759185
218	Phosphorylation	KYNKPSETVIPESVD HCCCCCCCCCCCCCC	28.24	29759185
248	Ubiquitination	HYYNCDFKMCYKLTS HHHCCCHHHEEECHH	18.14	-
254	Phosphorylation	FKMCYKLTSVVMEKD HHHEEECHHHHHHCC	18.47	21406692
255	Phosphorylation	KMCYKLTSVVMEKDP HHEEECHHHHHHCCC	24.13	21406692
260	Ubiquitination	LTSVVMEKDPFHASC CHHHHHHCCCCCCCC	53.24	-
322	Phosphorylation	KNEHARRYLSKATTL CCHHHHHHHHHCCCC	15.13	30177828
324	Phosphorylation	EHARRYLSKATTLEK HHHHHHHHHCCCCCC	16.00	21712546
325	Ubiquitination	HARRYLSKATTLEKT HHHHHHHHCCCCCCC	47.35	-
327	Phosphorylation	RRYLSKATTLEKTYG HHHHHHCCCCCCCCC	35.33	21712546
328	Phosphorylation	RYLSKATTLEKTYGP HHHHHCCCCCCCCCC	37.47	21712546
329	Ubiquitination	YLSKATTLEKTYGPA HHHHCCCCCCCCCCC	5.73	21890473
396	Phosphorylation	RFFSQALSIAPEDPF HHHHHHHHCCCCCCC	21.51	-
420	Phosphorylation	FQNGEWKTAEKWFLD EECCCEEHHHHHHHH	40.91	-
422 (in isoform 2)	Ubiquitination	-	56.93	21890473
423 (in isoform 1)	Ubiquitination	-	40.56	21890473
423	Ubiquitination	GEWKTAEKWFLDALE CCEEHHHHHHHHHHH	40.56	21890473
433	Ubiquitination	LDALEKIKAIGNEVT HHHHHHHHHHCCCCC	45.05	-
440	Phosphorylation	KAIGNEVTVDKWEPL HHHCCCCCCCCHHHH	19.46	-
443	Ubiquitination	GNEVTVDKWEPLLNN CCCCCCCCHHHHHHH	49.47	-
460	Ubiquitination	HVCRKLKKYAEALDY HHHHHHHHHHHHHHH	61.19	-
462	Ubiquitination	CRKLKKYAEALDYHR HHHHHHHHHHHHHHH	12.41	21890473
478	Ubiquitination	ALVLIPQNASTYSAI EEEEECCCCCHHHHH	30.42	21890473
490	Phosphorylation	SAIGYIHSLMGNFEN HHHHHHHHHHCCHHH	15.53	22817900
504 (in isoform 3)	Ubiquitination	-	17.43	21890473
520 (in isoform 3)	Ubiquitination	-	11.64	21890473
553	Ubiquitination	DFDVHTMKTLKNIIS CCCHHHHHHHHHHCC	52.43	-
555 (in isoform 2)	Ubiquitination	-	3.14	21890473
556	Ubiquitination	VHTMKTLKNIISPPW HHHHHHHHHHCCCCC	51.86	21890473
556 (in isoform 1)	Ubiquitination	-	51.86	21890473
560	Phosphorylation	KTLKNIISPPWDFRE HHHHHHCCCCCCHHH	22.55	22167270
571 (in isoform 2)	Ubiquitination	-	32.05	21890473
572	Ubiquitination	FREFEVEKQTAEETG HHHHCCCHHHHHHHC	59.11	2190698
572 (in isoform 1)	Ubiquitination	-	59.11	21890473
574	Phosphorylation	EFEVEKQTAEETGLT HHCCCHHHHHHHCCC	47.29	21406692
578	Phosphorylation	EKQTAEETGLTPLET CHHHHHHHCCCCCCC	29.06	26657352
581	Phosphorylation	TAEETGLTPLETSRK HHHHHCCCCCCCCCC	27.46	29255136
585	Phosphorylation	TGLTPLETSRKTPDS HCCCCCCCCCCCCCC	41.33	30108239
586	Phosphorylation	GLTPLETSRKTPDSR CCCCCCCCCCCCCCC	23.54	29255136
589	Phosphorylation	PLETSRKTPDSRPSL CCCCCCCCCCCCCCH	31.08	26074081
592	Phosphorylation	TSRKTPDSRPSLEET CCCCCCCCCCCHHHH	47.50	26074081
595	Phosphorylation	KTPDSRPSLEETFEI CCCCCCCCHHHHEEE	47.50	26074081
599	Phosphorylation	SRPSLEETFEIEMNE CCCCHHHHEEEEECH	19.72	7736578
607	Phosphorylation	FEIEMNESDMMLETS EEEEECHHHHEEEEC	26.29	27732954
613	Phosphorylation	ESDMMLETSMSDHST HHHHEEEECCCCCCC	26.26	27732954
614	Phosphorylation	SDMMLETSMSDHST- HHHEEEECCCCCCC-	13.60	27732954
616	Phosphorylation	MMLETSMSDHST--- HEEEECCCCCCC---	31.75	27732954
619	Phosphorylation	ETSMSDHST------ EECCCCCCC------	40.58	27732954
620	Phosphorylation	TSMSDHST------- ECCCCCCC-------	38.93	27732954

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
112	S	Phosphorylation	Kinase	CDK1	P06493	PSP
112	S	Phosphorylation	Kinase	PLK1	P53350	PSP
560	S	Phosphorylation	Kinase	CDK1	P06493	PSP
581	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
560	S	Phosphorylation		14657031
Phosphorylation on Ser-560 occurs specifically during mitosis.

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 CDC16_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPP5_MOUSE	Ppp5c	physical	9405394
CDC27_HUMAN	CDC27	physical	9405394
EP300_HUMAN	EP300	physical	16319895
CBP_HUMAN	CREBBP	physical	16319895
APC1_HUMAN	ANAPC1	physical	20360068
CDC20_HUMAN	CDC20	physical	20360068
APC7_HUMAN	ANAPC7	physical	20360068
CDC27_HUMAN	CDC27	physical	20733055
CCNB1_HUMAN	CCNB1	physical	20733055
MDC1_HUMAN	MDC1	physical	19826003
CDC27_HUMAN	CDC27	physical	22939629
CDC23_HUMAN	CDC23	physical	22939629
TRI33_HUMAN	TRIM33	physical	23160376
DNJA1_HUMAN	DNAJA1	physical	21988832
FRIH_HUMAN	FTH1	physical	21988832
DAB2_HUMAN	DAB2	physical	21988832
HINT1_HUMAN	HINT1	physical	21988832
XRCC5_HUMAN	XRCC5	physical	21988832
CDC26_HUMAN	CDC26	physical	21988832
CDC26_HUMAN	CDC26	physical	25416956
APC10_HUMAN	ANAPC10	physical	26344197
APC13_HUMAN	ANAPC13	physical	26344197
ANC2_HUMAN	ANAPC2	physical	26344197
APC4_HUMAN	ANAPC4	physical	26344197
APC5_HUMAN	ANAPC5	physical	26344197
CDC26_HUMAN	CDC26	physical	26344197
NP1L4_HUMAN	NAP1L4	physical	26344197
TAF3_HUMAN	TAF3	physical	26344197
ATP5J_HUMAN	ATP5J	physical	26496610
CDC20_HUMAN	CDC20	physical	26496610
CDC27_HUMAN	CDC27	physical	26496610
NEK2_HUMAN	NEK2	physical	26496610
P5CR1_HUMAN	PYCR1	physical	26496610
CDC23_HUMAN	CDC23	physical	26496610
APC10_HUMAN	ANAPC10	physical	26496610
B4GT7_HUMAN	B4GALT7	physical	26496610
FBX5_HUMAN	FBXO5	physical	26496610
ANC2_HUMAN	ANAPC2	physical	26496610
P5CR2_HUMAN	PYCR2	physical	26496610
APC4_HUMAN	ANAPC4	physical	26496610
FZR1_HUMAN	FZR1	physical	26496610
APC5_HUMAN	ANAPC5	physical	26496610
APC7_HUMAN	ANAPC7	physical	26496610
NSUN5_HUMAN	NSUN5	physical	26496610
APC1_HUMAN	ANAPC1	physical	26496610
APC16_HUMAN	ANAPC16	physical	26496610
SMCR8_HUMAN	SMCR8	physical	26496610
CDC26_HUMAN	CDC26	physical	26496610
CDC26_HUMAN	CDC26	physical	25723520
CDC27_HUMAN	CDC27	physical	24100295
ANC2_HUMAN	ANAPC2	physical	28514442
CDC26_HUMAN	CDC26	physical	28514442
APC4_HUMAN	ANAPC4	physical	28514442
TALD3_HUMAN	KIAA0586	physical	28514442
CDC23_HUMAN	CDC23	physical	28514442
APC5_HUMAN	ANAPC5	physical	28514442
CE295_HUMAN	CEP295	physical	28514442
APC1_HUMAN	ANAPC1	physical	28514442
STIL_HUMAN	STIL	physical	28514442
KRBA1_HUMAN	KRBA1	physical	28514442
CE350_HUMAN	CEP350	physical	28514442
4ET_HUMAN	EIF4ENIF1	physical	28514442
APC16_HUMAN	ANAPC16	physical	28514442
ZN318_HUMAN	ZNF318	physical	28514442
UBP54_HUMAN	USP54	physical	28514442
CE164_HUMAN	CEP164	physical	28514442
CDC27_HUMAN	CDC27	physical	28514442
YYAP1_HUMAN	YY1AP1	physical	28514442
SALL2_HUMAN	SALL2	physical	28514442
TTC8_HUMAN	TTC8	physical	28514442
RECQ4_HUMAN	RECQL4	physical	28514442
MYO5C_HUMAN	MYO5C	physical	28514442
ALMS1_HUMAN	ALMS1	physical	28514442
ZBTB5_HUMAN	ZBTB5	physical	28514442
HAUS8_HUMAN	HAUS8	physical	28514442
TRPS1_HUMAN	TRPS1	physical	28514442
DUS3L_HUMAN	DUS3L	physical	28514442
CN080_HUMAN	C14orf80	physical	28514442
TROAP_HUMAN	TROAP	physical	28514442
ZN644_HUMAN	ZNF644	physical	28514442
SMG8_HUMAN	SMG8	physical	28514442
IQCB1_HUMAN	IQCB1	physical	28514442
BUB1_HUMAN	BUB1	physical	28514442
SMG7_HUMAN	SMG7	physical	28514442
CO039_HUMAN	C15orf39	physical	28514442
PLCH1_HUMAN	PLCH1	physical	28514442
APC7_HUMAN	ANAPC7	physical	28514442
LONP2_HUMAN	LONP2	physical	28514442
RICTR_HUMAN	RICTOR	physical	28514442
P3C2A_HUMAN	PIK3C2A	physical	28514442
CP110_HUMAN	CCP110	physical	28514442
NCOR1_HUMAN	NCOR1	physical	28514442
HAUS6_HUMAN	HAUS6	physical	28514442
ERF_HUMAN	ERF	physical	28514442
PHLB3_HUMAN	PHLDB3	physical	28514442
MYO9A_HUMAN	MYO9A	physical	28514442
BCOR_HUMAN	BCOR	physical	28514442
DISC1_HUMAN	DISC1	physical	28514442
HAUS3_HUMAN	HAUS3	physical	28514442
SNX18_HUMAN	SNX18	physical	28514442
HOOK3_HUMAN	HOOK3	physical	28514442
CSR2B_HUMAN	CSRP2BP	physical	28514442
RAVR1_HUMAN	RAVER1	physical	28514442
TRI37_HUMAN	TRIM37	physical	28514442
ZN687_HUMAN	ZNF687	physical	28514442
ASPM_HUMAN	ASPM	physical	28514442
CEP97_HUMAN	CEP97	physical	28514442
IQGA3_HUMAN	IQGAP3	physical	28514442
IF4E2_HUMAN	EIF4E2	physical	28514442
TRI33_HUMAN	TRIM33	physical	28514442
HAUS7_HUMAN	HAUS7	physical	28514442
TASOR_HUMAN	FAM208A	physical	28514442
JMJD4_HUMAN	JMJD4	physical	28514442
FA83H_HUMAN	FAM83H	physical	28514442
MGAP_HUMAN	MGA	physical	28514442
HAUS5_HUMAN	HAUS5	physical	28514442
TIF1A_HUMAN	TRIM24	physical	28514442
ZN281_HUMAN	ZNF281	physical	28514442
HOOK1_HUMAN	HOOK1	physical	28514442
MKS1_HUMAN	MKS1	physical	28514442
GTSE1_HUMAN	GTSE1	physical	28514442
MA7D3_HUMAN	MAP7D3	physical	28514442
DHX35_HUMAN	DHX35	physical	28514442
BCD1_HUMAN	ZNHIT6	physical	28514442
YDJC_HUMAN	YDJC	physical	28514442
SAMD1_HUMAN	SAMD1	physical	28514442
ESPL1_HUMAN	ESPL1	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
MED12_HUMAN	MED12	physical	28514442
MLF1_HUMAN	MLF1	physical	28514442
P66B_HUMAN	GATAD2B	physical	28514442
ALG13_HUMAN	ALG13	physical	28514442
CDC27_HUMAN	CDC27	physical	27173435
CDC23_HUMAN	CDC23	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 CDC16_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-560, 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-560 AND THR-581, ANDMASS SPECTROMETRY.	18691976 [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-560, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND THR-581, ANDMASS SPECTROMETRY.	16565220 [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 SER-560 AND THR-581, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Mitotic regulation of the human anaphase-promoting complex byphosphorylation."; Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,Peters J.-M.; EMBO J. 22:6598-6609(2003). Cited for: PHOSPHORYLATION AT SER-112; SER-490; SER-560; THR-581; SER-595 ANDTHR-599.	14657031 [Abstract]
"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 THR-581, AND MASSSPECTROMETRY.	19690332 [Abstract]

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