dbPTM

CYBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CYBP_HUMAN
UniProt AC	Q9HB71
Protein Name	Calcyclin-binding protein
Gene Name	CACYBP
Organism	Homo sapiens (Human).
Sequence Length	228
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasmic at low calcium concentrations. In neuroblastoma cells, after a retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear fraction may be phosphorylated.
Protein Description	May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1)..
Protein Sequence	MASEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEIKNKMQQKSQKKAELLDNEKPAAVVAPITTGYTVKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKSYSMIVNNLLKPISVEGSSKKVKTDTVLILCRKKVENTRWDYLTQVEKECKEKEKPSYDTETDPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAKGDTEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASEELQKD ------CCCHHHHHH	26.16	19413330
3	Phosphorylation	-----MASEELQKDL -----CCCHHHHHHH	30.24	25159151
8	Acetylation	MASEELQKDLEEVKV CCCHHHHHHHHHHHH	76.53	19608861
8	Succinylation	MASEELQKDLEEVKV CCCHHHHHHHHHHHH	76.53	23954790
8	Ubiquitination	MASEELQKDLEEVKV CCCHHHHHHHHHHHH	76.53	19608861
14	Ubiquitination	QKDLEEVKVLLEKAT HHHHHHHHHHHHHHH	30.37	21890473
14	2-Hydroxyisobutyrylation	QKDLEEVKVLLEKAT HHHHHHHHHHHHHHH	30.37	-
14	Acetylation	QKDLEEVKVLLEKAT HHHHHHHHHHHHHHH	30.37	26822725
14	Ubiquitination	QKDLEEVKVLLEKAT HHHHHHHHHHHHHHH	30.37	21890473
14 (in isoform 1)	Ubiquitination	-	30.37	21890473
14 (in isoform 2)	Ubiquitination	-	30.37	21890473
19	2-Hydroxyisobutyrylation	EVKVLLEKATRKRVR HHHHHHHHHHHHHHH	55.84	-
19	Acetylation	EVKVLLEKATRKRVR HHHHHHHHHHHHHHH	55.84	19608861
19	Ubiquitination	EVKVLLEKATRKRVR HHHHHHHHHHHHHHH	55.84	19608861
30	Phosphorylation	KRVRDALTAEKSKIE HHHHHHHHHHHHHHH	34.19	29214152
33	2-Hydroxyisobutyrylation	RDALTAEKSKIETEI HHHHHHHHHHHHHHH	55.36	-
33	Acetylation	RDALTAEKSKIETEI HHHHHHHHHHHHHHH	55.36	23749302
33	Ubiquitination	RDALTAEKSKIETEI HHHHHHHHHHHHHHH	55.36	22053931
33 (in isoform 1)	Ubiquitination	-	55.36	21890473
34	Phosphorylation	DALTAEKSKIETEIK HHHHHHHHHHHHHHH	30.30	21712546
41	Acetylation	SKIETEIKNKMQQKS HHHHHHHHHHHHHHH	44.26	25953088
41	Ubiquitination	SKIETEIKNKMQQKS HHHHHHHHHHHHHHH	44.26	-
42	Acetylation	KIETEIKNKMQQKSQ HHHHHHHHHHHHHHH	51.17	19608861
42	Ubiquitination	KIETEIKNKMQQKSQ HHHHHHHHHHHHHHH	51.17	19608861
43	Ubiquitination	IETEIKNKMQQKSQK HHHHHHHHHHHHHHH	32.84	-
48	Phosphorylation	KNKMQQKSQKKAELL HHHHHHHHHHHHHHH	42.78	29978859
51	2-Hydroxyisobutyrylation	MQQKSQKKAELLDNE HHHHHHHHHHHHCCC	39.18	-
51	Acetylation	MQQKSQKKAELLDNE HHHHHHHHHHHHCCC	39.18	26051181
51	Ubiquitination	MQQKSQKKAELLDNE HHHHHHHHHHHHCCC	39.18	-
58	Ubiquitination	KAELLDNEKPAAVVA HHHHHCCCCCCEEEE	61.15	21890473
58	Ubiquitination	KAELLDNEKPAAVVA HHHHHCCCCCCEEEE	61.15	21890473
59	2-Hydroxyisobutyrylation	AELLDNEKPAAVVAP HHHHCCCCCCEEEEE	46.33	-
59	Acetylation	AELLDNEKPAAVVAP HHHHCCCCCCEEEEE	46.33	23954790
59	Ubiquitination	AELLDNEKPAAVVAP HHHHCCCCCCEEEEE	46.33	-
68	Phosphorylation	AAVVAPITTGYTVKI CEEEEEECCCEEEEE	17.07	28152594
69	Phosphorylation	AVVAPITTGYTVKIS EEEEEECCCEEEEEE	28.98	28152594
71	Phosphorylation	VAPITTGYTVKISNY EEEECCCEEEEEECC	13.28	28152594
72	Phosphorylation	APITTGYTVKISNYG EEECCCEEEEEECCC	19.37	28152594
74	Ubiquitination	ITTGYTVKISNYGWD ECCCEEEEEECCCCC	32.39	-
75	Acetylation	TTGYTVKISNYGWDQ CCCEEEEEECCCCCC	2.54	19608861
75	Ubiquitination	TTGYTVKISNYGWDQ CCCEEEEEECCCCCC	2.54	19608861
76	Phosphorylation	TGYTVKISNYGWDQS CCEEEEEECCCCCCC	20.48	28152594
78	Phosphorylation	YTVKISNYGWDQSDK EEEEEECCCCCCCCC	16.89	28152594
85	Ubiquitination	YGWDQSDKFVKIYIT CCCCCCCCEEEEEEE	58.25	21890473
85	Acetylation	YGWDQSDKFVKIYIT CCCCCCCCEEEEEEE	58.25	19608861
85	Malonylation	YGWDQSDKFVKIYIT CCCCCCCCEEEEEEE	58.25	26320211
85	Ubiquitination	YGWDQSDKFVKIYIT CCCCCCCCEEEEEEE	58.25	21890473
85 (in isoform 1)	Ubiquitination	-	58.25	21890473
90	Phosphorylation	SDKFVKIYITLTGVH CCCEEEEEEEEECCE	5.11	28152594
91	Ubiquitination	DKFVKIYITLTGVHQ CCEEEEEEEEECCEE	2.64	21890473
91	Ubiquitination	DKFVKIYITLTGVHQ CCEEEEEEEEECCEE	2.64	21890473
91	Acetylation	DKFVKIYITLTGVHQ CCEEEEEEEEECCEE	2.64	19608861
92	Phosphorylation	KFVKIYITLTGVHQV CEEEEEEEEECCEEC	10.99	28442448
96	Ubiquitination	IYITLTGVHQVPTEN EEEEEECCEECCCCC	2.10	21890473
96	Ubiquitination	IYITLTGVHQVPTEN EEEEEECCEECCCCC	2.10	21890473
112	Phosphorylation	QVHFTERSFDLLVKN EEEEEHHHHHEEEEC	19.51	21712546
118	Ubiquitination	RSFDLLVKNLNGKSY HHHHEEEECCCCCCE	56.54	21890473
118	Acetylation	RSFDLLVKNLNGKSY HHHHEEEECCCCCCE	56.54	19608861
118	Ubiquitination	RSFDLLVKNLNGKSY HHHHEEEECCCCCCE	56.54	21890473
118 (in isoform 1)	Ubiquitination	-	56.54	21890473
123	Ubiquitination	LVKNLNGKSYSMIVN EEECCCCCCEEHHHC	45.18	21890473
123	Ubiquitination	LVKNLNGKSYSMIVN EEECCCCCCEEHHHC	45.18	21890473
123 (in isoform 1)	Ubiquitination	-	45.18	21890473
125	Phosphorylation	KNLNGKSYSMIVNNL ECCCCCCEEHHHCCC	13.02	22817900
134	Acetylation	MIVNNLLKPISVEGS HHHCCCCCCCCCCCC	43.39	23954790
134	Ubiquitination	MIVNNLLKPISVEGS HHHCCCCCCCCCCCC	43.39	19608861
141	Phosphorylation	KPISVEGSSKKVKTD CCCCCCCCCCCCCCC	26.02	20729913
142	Phosphorylation	PISVEGSSKKVKTDT CCCCCCCCCCCCCCE	47.56	25627689
143	2-Hydroxyisobutyrylation	ISVEGSSKKVKTDTV CCCCCCCCCCCCCEE	64.38	-
143	Acetylation	ISVEGSSKKVKTDTV CCCCCCCCCCCCCEE	64.38	25953088
143	Ubiquitination	ISVEGSSKKVKTDTV CCCCCCCCCCCCCEE	64.38	21906983
144	Malonylation	SVEGSSKKVKTDTVL CCCCCCCCCCCCEEE	51.41	26320211
144	Ubiquitination	SVEGSSKKVKTDTVL CCCCCCCCCCCCEEE	51.41	-
146	2-Hydroxyisobutyrylation	EGSSKKVKTDTVLIL CCCCCCCCCCEEEEE	49.95	-
146	Acetylation	EGSSKKVKTDTVLIL CCCCCCCCCCEEEEE	49.95	27452117
146	Malonylation	EGSSKKVKTDTVLIL CCCCCCCCCCEEEEE	49.95	26320211
146	Ubiquitination	EGSSKKVKTDTVLIL CCCCCCCCCCEEEEE	49.95	-
146 (in isoform 1)	Ubiquitination	-	49.95	21890473
147	Phosphorylation	GSSKKVKTDTVLILC CCCCCCCCCEEEEEE	39.63	23882029
149	Phosphorylation	SKKVKTDTVLILCRK CCCCCCCEEEEEEEC	23.57	21712546
154	Glutathionylation	TDTVLILCRKKVENT CCEEEEEEECCHHHC	4.80	22555962
154	S-nitrosylation	TDTVLILCRKKVENT CCEEEEEEECCHHHC	4.80	2212679
157	Ubiquitination	VLILCRKKVENTRWD EEEEEECCHHHCCHH	35.11	-
162	Methylation	RKKVENTRWDYLTQV ECCHHHCCHHHHHHH	35.53	-
165	Phosphorylation	VENTRWDYLTQVEKE HHHCCHHHHHHHHHH	12.51	28152594
167	Phosphorylation	NTRWDYLTQVEKECK HCCHHHHHHHHHHHH	25.08	28152594
171	2-Hydroxyisobutyrylation	DYLTQVEKECKEKEK HHHHHHHHHHHHHCC	70.34	-
171	Acetylation	DYLTQVEKECKEKEK HHHHHHHHHHHHHCC	70.34	23749302
171	Ubiquitination	DYLTQVEKECKEKEK HHHHHHHHHHHHHCC	70.34	-
173	Glutathionylation	LTQVEKECKEKEKPS HHHHHHHHHHHCCCC	11.61	22555962
176	Acetylation	VEKECKEKEKPSYDT HHHHHHHHCCCCCCC	57.44	25953088
176	Ubiquitination	VEKECKEKEKPSYDT HHHHHHHHCCCCCCC	57.44	-
178	Acetylation	KECKEKEKPSYDTET HHHHHHCCCCCCCCC	50.78	25953088
178	Ubiquitination	KECKEKEKPSYDTET HHHHHHCCCCCCCCC	50.78	21906983
178 (in isoform 1)	Ubiquitination	-	50.78	21890473
180	Phosphorylation	CKEKEKPSYDTETDP HHHHCCCCCCCCCCC	46.86	28796482
181	Phosphorylation	KEKEKPSYDTETDPS HHHCCCCCCCCCCCC	35.10	28796482
183	Phosphorylation	KEKPSYDTETDPSEG HCCCCCCCCCCCCCH	32.33	28796482
185	Ubiquitination	KPSYDTETDPSEGLM CCCCCCCCCCCCHHH	56.13	21890473
185	Ubiquitination	KPSYDTETDPSEGLM CCCCCCCCCCCCHHH	56.13	21890473
185	Phosphorylation	KPSYDTETDPSEGLM CCCCCCCCCCCCHHH	56.13	30576142
188	Phosphorylation	YDTETDPSEGLMNVL CCCCCCCCCHHHHHH	47.29	30576142
192	Sulfoxidation	TDPSEGLMNVLKKIY CCCCCHHHHHHHHHH	4.85	30846556
196	2-Hydroxyisobutyrylation	EGLMNVLKKIYEDGD CHHHHHHHHHHCCCC	32.61	-
196	Acetylation	EGLMNVLKKIYEDGD CHHHHHHHHHHCCCC	32.61	25953088
196	Ubiquitination	EGLMNVLKKIYEDGD CHHHHHHHHHHCCCC	32.61	21906983
196 (in isoform 1)	Ubiquitination	-	32.61	21890473
197	Ubiquitination	GLMNVLKKIYEDGDD HHHHHHHHHHCCCCH	46.49	21906983
197 (in isoform 1)	Ubiquitination	-	46.49	21890473
199	Phosphorylation	MNVLKKIYEDGDDDM HHHHHHHHCCCCHHH	19.49	27273156
206	Sulfoxidation	YEDGDDDMKRTINKA HCCCCHHHHHHHHHH	3.99	30846556
207	Acetylation	EDGDDDMKRTINKAW CCCCHHHHHHHHHHH	54.08	26051181
207	Ubiquitination	EDGDDDMKRTINKAW CCCCHHHHHHHHHHH	54.08	21906983
207 (in isoform 1)	Ubiquitination	-	54.08	21890473
209	Phosphorylation	GDDDMKRTINKAWVE CCHHHHHHHHHHHHH	24.31	30576142
212	Ubiquitination	DMKRTINKAWVESRE HHHHHHHHHHHHHHH	39.51	21890473
212	Acetylation	DMKRTINKAWVESRE HHHHHHHHHHHHHHH	39.51	25953088
212	Ubiquitination	DMKRTINKAWVESRE HHHHHHHHHHHHHHH	39.51	21906983
212 (in isoform 1)	Ubiquitination	-	39.51	21890473
220	Ubiquitination	AWVESREKQAKGDTE HHHHHHHHHHCCCCC	55.21	-
223	Ubiquitination	ESREKQAKGDTEF-- HHHHHHHCCCCCC--	55.62	-

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
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:20181957

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SKP1_HUMAN	SKP1	physical	11389839
SIAH1_HUMAN	SIAH1	physical	11389839
SIAH1_HUMAN	SIAH1	physical	16085652
CYBP_HUMAN	CACYBP	physical	16085652
MK01_HUMAN	MAPK1	physical	21110948
CYBP_HUMAN	CACYBP	physical	22295074
S10A6_HUMAN	S100A6	physical	22295074
SKP1_HUMAN	SKP1	physical	22295074
SIAH1_HUMAN	SIAH1	physical	22295074
ROA0_HUMAN	HNRNPA0	physical	22939629
BEX3_HUMAN	NGFRAP1	physical	21988832
CD8A_HUMAN	CD8A	physical	21988832
PINX1_HUMAN	PINX1	physical	21988832
PRDX1_HUMAN	PRDX1	physical	22863883
PRDX2_HUMAN	PRDX2	physical	22863883
TPD52_HUMAN	TPD52	physical	22863883
UBC9_HUMAN	UBE2I	physical	24078263
RNF41_HUMAN	RNF41	physical	25036637
CARM1_HUMAN	CARM1	physical	25036637
ANXA2_HUMAN	ANXA2	physical	26344197
NAA20_HUMAN	NAA20	physical	26344197
NAA25_HUMAN	NAA25	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
UBP19_HUMAN	USP19	physical	26344197
CTNB1_HUMAN	CTNNB1	physical	25241761
TBL1X_HUMAN	TBL1X	physical	25241761
SIAH1_HUMAN	SIAH1	physical	25241761
SKP1_HUMAN	SKP1	physical	27099442
SKP1_HUMAN	SKP1	physical	28196083

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 CYBP_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, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-19; LYS-85; LYS-118AND LYS-134, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-209, AND MASSSPECTROMETRY.	17287340 [Abstract]