dbPTM

CRTC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRTC1_HUMAN
UniProt AC	Q6UUV9
Protein Name	CREB-regulated transcription coactivator 1
Gene Name	CRTC1 {ECO:0000312\|HGNC:HGNC:16062}
Organism	Homo sapiens (Human).
Sequence Length	634
Subcellular Localization	Cytoplasm . Nucleus . Cytoplasmic when phosphorylated by SIK or AMPK and when sequestered by 14-3-3 proteins (PubMed:16817901). Translocated to the nucleus on Ser-151 dephosphorylation, instigated by a number of factors including calcium ion and cAMP
Protein Description	Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells. In the hippocampus, involved in late-phase long-term potentiation (L-LTP) maintenance at the Schaffer collateral-CA1 synapses. May be required for dendritic growth of developing cortical neurons (By similarity). In concert with SIK1, regulates the light-induced entrainment of the circadian clock. In response to light stimulus, coactivates the CREB-mediated transcription of PER1 which plays an important role in the photic entrainment of the circadian clock.; (Microbial infection) Plays a role of coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR)..
Protein Sequence	MATSNNPRKFSEKIALHNQKQAEETAAFEEVMKDLSLTRAARLQLQKSQYLQLGPSRGQYYGGSLPNVNQIGSGTMDLPFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLSVDKHGRQADSCPYGTMYLSPPADTSWRRTNSDSALHQSTMTPTQPESFSSGSQDVHQKRVLLLTVPGMEETTSEADKNLSKQAWDTKKTGSRPKSCEVPGINIFPSADQENTTALIPATHNTGGSLPDLTNIHFPSPLPTPLDPEEPTFPALSSSSSTGNLAANLTHLGIGGAGQGMSTPGSSPQHRPAGVSPLSLSTEARRQQASPTLSPLSPITQAVAMDALSLEQQLPYAFFTQAGSQQPPPQPQPPPPPPPASQQPPPPPPPQAPVRLPPGGPLLPSASLTRGPQPPPLAVTVPSSLPQSPPENPGQPSMGIDIASAPALQQYRTSAGSPANQSPTSPVSNQGFSPGSSPQHTSTLGSVFGDAYYEQQMAARQANALSHQLEQFNMMENAISSSSLYSPGSTLNYSQAAMMGLTGSHGSLPDSQQLGYASHSGIPNIILTVTGESPPSLSKELTSSLAGVGDVSFDSDSQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	SNNPRKFSEKIALHN CCCHHHHHHHHHHHC	40.80	24719451
11 (in isoform 2)	Phosphorylation	-	40.80	24719451
13	Ubiquitination	NPRKFSEKIALHNQK CHHHHHHHHHHHCHH	31.89	29967540
36	Phosphorylation	EEVMKDLSLTRAARL HHHHHHHHHHHHHHH	37.52	24719451
47	Ubiquitination	AARLQLQKSQYLQLG HHHHHHHHHHCEEEC	48.39	22817900
47 (in isoform 3)	Ubiquitination	-	48.39	21890473
47 (in isoform 1)	Ubiquitination	-	48.39	21890473
47 (in isoform 2)	Ubiquitination	-	48.39	21890473
48 (in isoform 2)	Phosphorylation	-	15.88	27642862
48	Phosphorylation	ARLQLQKSQYLQLGP HHHHHHHHHCEEECC	15.88	28796482
50	Phosphorylation	LQLQKSQYLQLGPSR HHHHHHHCEEECCCC	11.96	28796482
50 (in isoform 2)	Phosphorylation	-	11.96	27642862
60	Phosphorylation	LGPSRGQYYGGSLPN ECCCCCCCCCCCCCC	13.60	28450419
61	Phosphorylation	GPSRGQYYGGSLPNV CCCCCCCCCCCCCCC	13.71	28450419
64 (in isoform 2)	Phosphorylation	-	35.97	28348404
64	Phosphorylation	RGQYYGGSLPNVNQI CCCCCCCCCCCCCEE	35.97	28674151
73	Phosphorylation	PNVNQIGSGTMDLPF CCCCEECCCCCCCCC	32.49	28464451
75	Phosphorylation	VNQIGSGTMDLPFQT CCEECCCCCCCCCCC	14.81	28464451
82	Phosphorylation	TMDLPFQTPFQSSGL CCCCCCCCCCCCCCC	26.84	27080861
103	Methylation	RHHGLVDRVYRERGR HHHCHHHHHHHHCCC	21.64	115918753
113	Phosphorylation	RERGRLGSPHRRPLS HHCCCCCCCCCCCCC	23.33	23401153
120	Phosphorylation	SPHRRPLSVDKHGRQ CCCCCCCCCCCCCCC	30.84	23403867
123	Acetylation	RRPLSVDKHGRQADS CCCCCCCCCCCCCCC	45.89	11792777
129 (in isoform 2)	Phosphorylation	-	42.29	24719451
130	Phosphorylation	KHGRQADSCPYGTMY CCCCCCCCCCCCCEE	21.73	28857561
136 (in isoform 2)	Phosphorylation	-	2.48	24719451
137	Phosphorylation	SCPYGTMYLSPPADT CCCCCCEEECCCCCC	12.13	28348404
139	Phosphorylation	PYGTMYLSPPADTSW CCCCEEECCCCCCCC	16.02	25159151
144	Phosphorylation	YLSPPADTSWRRTNS EECCCCCCCCCCCCC	32.09	26074081
145	Phosphorylation	LSPPADTSWRRTNSD ECCCCCCCCCCCCCC	21.09	26074081
146 (in isoform 2)	Phosphorylation	-	8.89	24719451
149	Phosphorylation	ADTSWRRTNSDSALH CCCCCCCCCCCCCCC	30.42	23927012
151	Phosphorylation	TSWRRTNSDSALHQS CCCCCCCCCCCCCCC	32.12	23927012
153	Phosphorylation	WRRTNSDSALHQSTM CCCCCCCCCCCCCCC	32.33	23401153
155 (in isoform 2)	Phosphorylation	-	4.35	24719451
158	Phosphorylation	SDSALHQSTMTPTQP CCCCCCCCCCCCCCC	14.92	30278072
159	Phosphorylation	DSALHQSTMTPTQPE CCCCCCCCCCCCCCC	20.63	23927012
161	Phosphorylation	ALHQSTMTPTQPESF CCCCCCCCCCCCCCC	24.23	23927012
163	Phosphorylation	HQSTMTPTQPESFSS CCCCCCCCCCCCCCC	47.81	23927012
165 (in isoform 2)	Phosphorylation	-	41.50	24719451
167	Phosphorylation	MTPTQPESFSSGSQD CCCCCCCCCCCCCCC	36.79	23927012
167 (in isoform 2)	Phosphorylation	-	36.79	24719451
169	Phosphorylation	PTQPESFSSGSQDVH CCCCCCCCCCCCCHH	42.97	23927012
169 (in isoform 2)	Phosphorylation	-	42.97	27251275
170	Phosphorylation	TQPESFSSGSQDVHQ CCCCCCCCCCCCHHC	40.22	23927012
172	Phosphorylation	PESFSSGSQDVHQKR CCCCCCCCCCHHCCE	25.75	17525332
183 (in isoform 2)	Phosphorylation	-	3.87	24719451
186 (in isoform 2)	Phosphorylation	-	31.04	27251275
186	Phosphorylation	RVLLLTVPGMEETTS EEEEEECCCCHHHCC	31.04	32142685
215	Phosphorylation	KTGSRPKSCEVPGIN CCCCCCCCCCCCCEE	20.42	-
239	Phosphorylation	TTALIPATHNTGGSL CCEEEECCCCCCCCC	15.42	26074081
242	Phosphorylation	LIPATHNTGGSLPDL EEECCCCCCCCCCCC	35.00	26074081
245	Phosphorylation	ATHNTGGSLPDLTNI CCCCCCCCCCCCCCC	37.77	26074081
312	Phosphorylation	QHRPAGVSPLSLSTE CCCCCCCCCCCCCHH	21.14	29255136
315	Phosphorylation	PAGVSPLSLSTEARR CCCCCCCCCCHHHHH	24.53	27732954
317	Phosphorylation	GVSPLSLSTEARRQQ CCCCCCCCHHHHHHH	22.33	27732954
318	Phosphorylation	VSPLSLSTEARRQQA CCCCCCCHHHHHHHC	38.67	27732954
330	Phosphorylation	QQASPTLSPLSPITQ HHCCCCCCCCCHHHH	26.69	-
333	Phosphorylation	SPTLSPLSPITQAVA CCCCCCCCHHHHHHH	20.03	21552520
401	Phosphorylation	PGGPLLPSASLTRGP CCCCCCCCHHCCCCC	30.38	28555341
403	Phosphorylation	GPLLPSASLTRGPQP CCCCCCHHCCCCCCC	34.31	28555341
419	Phosphorylation	PLAVTVPSSLPQSPP CEEEECCCCCCCCCC	39.92	28348404
420	Phosphorylation	LAVTVPSSLPQSPPE EEEECCCCCCCCCCC	37.69	29496963
424	Phosphorylation	VPSSLPQSPPENPGQ CCCCCCCCCCCCCCC	40.25	32142685
436 (in isoform 2)	Phosphorylation	-	2.31	27251275
440	Phosphorylation	SMGIDIASAPALQQY CCCCCCCCCHHHHHH	34.81	32142685
460	Phosphorylation	SPANQSPTSPVSNQG CCCCCCCCCCCCCCC	51.41	28348404
461	Phosphorylation	PANQSPTSPVSNQGF CCCCCCCCCCCCCCC	27.04	28348404
464	Phosphorylation	QSPTSPVSNQGFSPG CCCCCCCCCCCCCCC	27.16	28348404
469	Phosphorylation	PVSNQGFSPGSSPQH CCCCCCCCCCCCCCC	34.87	28348404
472	Phosphorylation	NQGFSPGSSPQHTST CCCCCCCCCCCCHHH	42.08	28348404
473	Phosphorylation	QGFSPGSSPQHTSTL CCCCCCCCCCCHHHH	34.20	28348404
477	Phosphorylation	PGSSPQHTSTLGSVF CCCCCCCHHHHHHHH	20.40	28348404
478	Phosphorylation	GSSPQHTSTLGSVFG CCCCCCHHHHHHHHH	21.36	28348404
479	Phosphorylation	SSPQHTSTLGSVFGD CCCCCHHHHHHHHHH	35.97	28348404
480 (in isoform 2)	Phosphorylation	-	4.89	27251275
482	Phosphorylation	QHTSTLGSVFGDAYY CCHHHHHHHHHHHHH	19.86	28348404
488	Phosphorylation	GSVFGDAYYEQQMAA HHHHHHHHHHHHHHH	16.57	28348404
494 (in isoform 2)	Phosphorylation	-	8.65	27251275
540	Phosphorylation	AMMGLTGSHGSLPDS HHCCCCCCCCCCCHH	21.31	26074081
543	Phosphorylation	GLTGSHGSLPDSQQL CCCCCCCCCCHHHHH	31.16	26074081
564	Phosphorylation	GIPNIILTVTGESPP CCCCEEEEEECCCCC	12.96	26657352
566	Phosphorylation	PNIILTVTGESPPSL CCEEEEEECCCCCCC	29.96	26657352
569	Phosphorylation	ILTVTGESPPSLSKE EEEEECCCCCCCCHH	43.38	26074081
571 (in isoform 3)	Phosphorylation	-	58.12	-
572	Phosphorylation	VTGESPPSLSKELTS EECCCCCCCCHHHHH	48.97	26074081
574	Phosphorylation	GESPPSLSKELTSSL CCCCCCCCHHHHHHH	28.55	26074081
578	Phosphorylation	PSLSKELTSSLAGVG CCCCHHHHHHHCCCC	19.84	27732954
579	Phosphorylation	SLSKELTSSLAGVGD CCCHHHHHHHCCCCC	35.66	27732954
580	Phosphorylation	LSKELTSSLAGVGDV CCHHHHHHHCCCCCC	19.60	27732954
588	Phosphorylation	LAGVGDVSFDSDSQF HCCCCCCCCCCCCCC	28.24	27732954
591	Phosphorylation	VGDVSFDSDSQFPLD CCCCCCCCCCCCCHH	36.83	27732954
593	Phosphorylation	DVSFDSDSQFPLDEL CCCCCCCCCCCHHHC	37.36	27732954
604 (in isoform 2)	Phosphorylation	-	30.62	27251275

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
151	S	Phosphorylation	Kinase	SIK1	P57059	Uniprot
151	S	Phosphorylation	Kinase	SIK2	Q9H0K1	Uniprot
151	S	Phosphorylation	Kinase	LKB1	Q15831	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
151	S	Phosphorylation		16817901
Phosphorylation/dephosphorylation states of Ser-151 are required for regulating transduction of CREB activity.

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 CRTC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
M3K1_HUMAN	MAP3K1	physical	18784253

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 CRTC1_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-151 AND THR-161, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-172, ANDMASS SPECTROMETRY.	17525332 [Abstract]
"Silencing the constitutive active transcription factor CREB by theLKB1-SIK signaling cascade."; Katoh Y., Takemori H., Lin X.-Z., Tamura M., Muraoka M., Satoh T.,Tsuchiya Y., Min L., Doi J., Miyauchi A., Witters L.A., Nakamura H.,Okamoto M.; FEBS J. 273:2730-2748(2006). Cited for: FUNCTION, PHOSPHORYLATION AT SER-151, AND SUBCELLULAR LOCATION.	16817901 [Abstract]

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