CRTC1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CRTC1_MOUSE
• UniProt AC: Q68ED7
• Protein Name: CREB-regulated transcription coactivator 1
• Gene Name: Crtc1 {ECO:0000312|MGI:MGI:2142523}
• Organism: Mus musculus (Mouse).
• Sequence Length: 630
• Subcellular Localization: Cytoplasm . Nucleus . Cytoplasmic when phosphorylated by SIK or AMPK and when sequestered by 14-3-3 proteins (By similarity). Translocated to the nucleus on Ser-151 dephosphorylation, instigated by a number of factors including calcium ion and cAMP l
• 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 (By similarity). 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. 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..
• Protein Sequence: MATSNNPRKFSEKIALHNQKQAEETAAFEEVMKDLSLTRAARLQLQKSQYLQLGPSRGQYYGGSLPNVNQIGSSSVDLAFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLSVDKHGRQADSCPYGTVYLSPPADTSWRRTNSDSALHQSTMTPSQAESFTGGSQDAHQKRVLLLTVPGMEDTGAETDKTLSKQSWDSKKAGSRPKSCEVPGINIFPSADQENTTALIPATHNTGGSLPDLTNIHFPSPLPTPLDPEEPPFPALTSSSSTGSLAHLGVGGAGQGMNTPSSSPQHRPAVVSPLSLSTEARRQQAQQVSPTLSPLSPITQAVAMDALSLEQQLPYAFFTQTGSQQPPPQPQPPPPPPPVSQQQPPPPQVSVGLPQGGPLLPSASLTRGPQLPPLSVTVPSTLPQSPTENPGQSPMGIDATSAPALQYRTSAGSPATQSPTSPVSNQGFSPGSSPQHTSTLGSVFGDAYYEQQMTARQANALSRQLEQFNMMENAISSSSLYNPGSTLNYSQAAMMGLSGSHGGLQDPQQLGYTGHGGIPNIILTVTGESPPSLSKELSSTLAGVSDVSFDSDHQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL

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
48	Phosphorylation	ARLQLQKSQYLQLGP HHHHHHHHHCEEECC	15.88	25338131
60	Phosphorylation	LGPSRGQYYGGSLPN ECCCCCCCCCCCCCC	13.60	23984901
61	Phosphorylation	GPSRGQYYGGSLPNV CCCCCCCCCCCCCCH	13.71	23984901
64	Phosphorylation	RGQYYGGSLPNVNQI CCCCCCCCCCCHHHC	35.97	27087446
73	Phosphorylation	PNVNQIGSSSVDLAF CCHHHCCCCCCEEEE	22.52	23984901
74	Phosphorylation	NVNQIGSSSVDLAFQ CHHHCCCCCCEEEEC	29.21	23984901
75	Phosphorylation	VNQIGSSSVDLAFQT HHHCCCCCCEEEECC	22.73	26745281
82	Phosphorylation	SVDLAFQTPFQSSGL CCEEEECCCCCCCCC	21.44	26643407
113	Phosphorylation	RERGRLGSPHRRPLS HHCCCCCCCCCCCCC	23.33	26824392
120	Phosphorylation	SPHRRPLSVDKHGRQ CCCCCCCCCCCCCCC	30.84	22324799
130	Phosphorylation	KHGRQADSCPYGTVY CCCCCCCCCCCCCEE	21.73	26643407
133	Phosphorylation	RQADSCPYGTVYLSP CCCCCCCCCCEEECC	29.74	29514104
135	Phosphorylation	ADSCPYGTVYLSPPA CCCCCCCCEEECCCC	10.51	26643407
137	Phosphorylation	SCPYGTVYLSPPADT CCCCCCEEECCCCCC	10.99	-
139	Phosphorylation	PYGTVYLSPPADTSW CCCCEEECCCCCCCC	15.91	26745281
149	Phosphorylation	ADTSWRRTNSDSALH CCCCCCCCCCCCCHH	30.42	27087446
151	Phosphorylation	TSWRRTNSDSALHQS CCCCCCCCCCCHHHC	32.12	27087446
153	Phosphorylation	WRRTNSDSALHQSTM CCCCCCCCCHHHCCC	32.33	27087446
158	Phosphorylation	SDSALHQSTMTPSQA CCCCHHHCCCCHHHH	14.92	26745281
159	Phosphorylation	DSALHQSTMTPSQAE CCCHHHCCCCHHHHH	20.63	26745281
161	Phosphorylation	ALHQSTMTPSQAESF CHHHCCCCHHHHHHH	21.63	27742792
163	Phosphorylation	HQSTMTPSQAESFTG HHCCCCHHHHHHHCC	32.62	21659605
167	Phosphorylation	MTPSQAESFTGGSQD CCHHHHHHHCCCCCC	30.99	25777480
169	Phosphorylation	PSQAESFTGGSQDAH HHHHHHHCCCCCCHH	50.33	18846507
172	Phosphorylation	AESFTGGSQDAHQKR HHHHCCCCCCHHCCE	26.65	26060331
308	Phosphorylation	QHRPAVVSPLSLSTE CCCCCCCCCCCCCHH	17.33	26824392
311	Phosphorylation	PAVVSPLSLSTEARR CCCCCCCCCCHHHHH	24.53	26643407
313	Phosphorylation	VVSPLSLSTEARRQQ CCCCCCCCHHHHHHH	22.33	26643407
314	Phosphorylation	VSPLSLSTEARRQQA CCCCCCCHHHHHHHH	38.67	26643407
411	Phosphorylation	GPQLPPLSVTVPSTL CCCCCCCEEECCCCC	22.86	26643407
413	Phosphorylation	QLPPLSVTVPSTLPQ CCCCCEEECCCCCCC	24.27	23649490
416	Phosphorylation	PLSVTVPSTLPQSPT CCEEECCCCCCCCCC	37.93	26643407
417	Phosphorylation	LSVTVPSTLPQSPTE CEEECCCCCCCCCCC	36.07	26643407
417	O-linked_Glycosylation	LSVTVPSTLPQSPTE CEEECCCCCCCCCCC	36.07	22517741
421	Phosphorylation	VPSTLPQSPTENPGQ CCCCCCCCCCCCCCC	31.67	26643407
423	Phosphorylation	STLPQSPTENPGQSP CCCCCCCCCCCCCCC	54.35	27087446
429	Phosphorylation	PTENPGQSPMGIDAT CCCCCCCCCCCCCCC	23.83	26643407
436	Phosphorylation	SPMGIDATSAPALQY CCCCCCCCCCCCCCC	22.98	26643407
437	Phosphorylation	PMGIDATSAPALQYR CCCCCCCCCCCCCCC	33.69	26643407
443	Phosphorylation	TSAPALQYRTSAGSP CCCCCCCCCCCCCCC	19.39	26643407
565	Phosphorylation	ILTVTGESPPSLSKE EEEEECCCCCCCCHH	43.38	25338131
581	Phosphorylation	SSTLAGVSDVSFDSD HHHHCCCCCCCCCCC	31.23	26643407
584	Phosphorylation	LAGVSDVSFDSDHQF HCCCCCCCCCCCCCC	28.46	26643407
587	Phosphorylation	VSDVSFDSDHQFPLD CCCCCCCCCCCCCHH	34.67	26643407

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CRTC1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
151	S	Phosphorylation	Phosphorylation/dephosphorylation states of Ser-151 are required for regulating transduction of CREB activity.	21183079

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CRTC1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CRTC1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.