CACO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CACO1_HUMAN
• UniProt AC: Q9P1Z2
• Protein Name: Calcium-binding and coiled-coil domain-containing protein 1
• Gene Name: CALCOCO1
• Organism: Homo sapiens (Human).
• Sequence Length: 691
• Subcellular Localization: Cytoplasm. Nucleus. Shuttles between nucleus and cytoplasm..
• Protein Description: Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions (By similarity). In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. [PubMed: 24245781; Seems to enhance inorganic pyrphosphatase thus activating phosphogluomutase (PMG Probably functions as component of the calphoglin complex, which is involved in linking cellular metabolism (phosphate and glucose metabolism) with other core functions including protein synthesis and degradation, calcium signaling and cell growth.]
• Protein Sequence: MEESPLSRAPSRGGVNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRDYHTFVWSSVPESTTDGSPIHTSVQFQASYLPKPGAQLYQFRYVNRQGQVCGQSPPFQFREPRPMDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVGLSCPAALTDSEDESPEDMRLPPYGLCERGDPGSSPAGPREASPLVVISQPAPISPHLSGPAEDSSSDSEAEDEKSVLMAAVQSGGEEANLLLPELGSAFYDMASGFTVGTLSETSTGGPATPTWKECPICKERFPAESDKDALEDHMDGHFFFSTQDPFTFE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MEESPLSRAPS ----CCCCCCCCCCC	20.17	22199227
7	Phosphorylation	-MEESPLSRAPSRGG -CCCCCCCCCCCCCC	29.76	23186163
11	Phosphorylation	SPLSRAPSRGGVNFL CCCCCCCCCCCCCCE	42.44	29523821
29	Sumoylation	RTYIPNTKVECHYTL EEECCCCCEEEEEEC	42.55	-
29	Sumoylation	RTYIPNTKVECHYTL EEECCCCCEEEEEEC	42.55	-
156	Phosphorylation	LQNQLDESQQERNDL HHHHCCHHHHHHHHH	36.51	28555341
243	Ubiquitination	DIQTISEKVLTKEVE HHHHHHHHHCCCHHH	35.44	-
247	Ubiquitination	ISEKVLTKEVELDRL HHHHHCCCHHHHHHH	56.45	-
273	Ubiquitination	EKLLGQLKEVQADKE HHHHHHHHHHHCCHH	48.21	-
325	Malonylation	KDKVAQMKDTLGQAQ HHHHHHHHHHHHHHH	35.17	26320211
342	Ubiquitination	VAELEPLKEQLRGAQ HHHHHHHHHHHHHHH	54.88	-
346	Methylation	EPLKEQLRGAQELAA HHHHHHHHHHHHHHH	37.79	-
358	Ubiquitination	LAASSQQKATLLGEE HHHHHHHHHHHHHHH	35.38	-
418	Phosphorylation	ERAGLLQSVEAEKDK HHHCHHHHHHHHHHH	23.15	24719451
460	Phosphorylation	ELAREKDSSLVQLSE HHHHHCCCCCHHHCH	36.32	28634120
461	Phosphorylation	LAREKDSSLVQLSES HHHHCCCCCHHHCHH	42.57	28634120
466	Phosphorylation	DSSLVQLSESKRELT CCCCHHHCHHHHHHH	23.80	21815630
468	Phosphorylation	SLVQLSESKRELTEL CCHHHCHHHHHHHHH	33.37	25627689
477	Phosphorylation	RELTELRSALRVLQK HHHHHHHHHHHHHHH	44.26	-
493	Ubiquitination	KEQLQEEKQELLEYM HHHHHHHHHHHHHHH	48.60	-
531	Phosphorylation	EEAAVGLSCPAALTD HHHHHCCCCCCCCCC	16.48	28348404
537	Phosphorylation	LSCPAALTDSEDESP CCCCCCCCCCCCCCC	32.52	28348404
539	Phosphorylation	CPAALTDSEDESPED CCCCCCCCCCCCCCC	41.53	28348404
562	Phosphorylation	CERGDPGSSPAGPRE CCCCCCCCCCCCCCC	38.24	29255136
563	Phosphorylation	ERGDPGSSPAGPREA CCCCCCCCCCCCCCC	25.37	29255136
571	Phosphorylation	PAGPREASPLVVISQ CCCCCCCCCEEEEEC	17.64	-
650	Phosphorylation	TSTGGPATPTWKECP CCCCCCCCCCCCCCC	25.12	-

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	SMURF1	Q9HCE7	PMID:20804422

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CACO1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CACO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH3G3_HUMAN	SH3GL3	physical	16169070
EP300_HUMAN	EP300	physical	16717280
CTNB1_HUMAN	CTNNB1	genetic	16931570
EP300_HUMAN	EP300	physical	16931570
A4_HUMAN	APP	physical	21832049
GRIK2_HUMAN	GRIK2	physical	21988832
TBC15_HUMAN	TBC1D15	physical	25416956
F161A_HUMAN	FAM161A	physical	25416956
CEP19_HUMAN	CEP19	physical	25416956
C19L2_HUMAN	CWF19L2	physical	25416956

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.