dbPTM

CRTC3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRTC3_HUMAN
UniProt AC	Q6UUV7
Protein Name	CREB-regulated transcription coactivator 3
Gene Name	CRTC3
Organism	Homo sapiens (Human).
Sequence Length	619
Subcellular Localization	Nucleus . Cytoplasm . Appears to be mainly nuclear.
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 PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR)..
Protein Sequence	MAASPGSGSANPRKFSEKIALHTQRQAEETRAFEQLMTDLTLSRVQFQKLQQLRLTQYHGGSLPNVSQLRSSASEFQPSFHQADNVRGTRHHGLVERPSRNRFHPLHRRSGDKPGRQFDGSAFGANYSSQPLDESWPRQQPPWKDEKHPGFRLTSALNRTNSDSALHTSALSTKPQDPYGGGGQSAWPAPYMGFCDGENNGHGEVASFPGPLKEENLLNVPKPLPKQLWETKEIQSLSGRPRSCDVGGGNAFPHNGQNLGLSPFLGTLNTGGSLPDLTNLHYSTPLPASLDTTDHHFGSMSVGNSVNNIPAAMTHLGIRSSSGLQSSRSNPSIQATLNKTVLSSSLNNHPQTSVPNASALHPSLRLFSLSNPSLSTTNLSGPSRRRQPPVSPLTLSPGPEAHQGFSRQLSSTSPLAPYPTSQMVSSDRSQLSFLPTEAQAQVSPPPPYPAPQELTQPLLQQPRAPEAPAQQPQAASSLPQSDFQLLPAQGSSLTNFFPDVGFDQQSMRPGPAFPQQVPLVQQGSRELQDSFHLRPSPYSNCGSLPNTILPEDSSTSLFKDLNSALAGLPEVSLNVDTPFPLEEELQIEPLSLDGLNMLSDSSMGLLDPSVEETFRADRL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAASPGSGSAN ----CCCCCCCCCCC	21.91	29255136
7	Phosphorylation	-MAASPGSGSANPRK -CCCCCCCCCCCHHH	32.72	23186163
9	Phosphorylation	AASPGSGSANPRKFS CCCCCCCCCCHHHHH	26.94	23186163
14	Sumoylation	SGSANPRKFSEKIAL CCCCCHHHHHHHHHH	55.27	-
16	Phosphorylation	SANPRKFSEKIALHT CCCHHHHHHHHHHHH	40.80	24719451
18	Sumoylation	NPRKFSEKIALHTQR CHHHHHHHHHHHHHH	31.89	-
18	Sumoylation	NPRKFSEKIALHTQR CHHHHHHHHHHHHHH	31.89	-
18	Ubiquitination	NPRKFSEKIALHTQR CHHHHHHHHHHHHHH	31.89	-
41	Phosphorylation	EQLMTDLTLSRVQFQ HHHHHHHHHHHHHHH	26.04	24719451
56	Phosphorylation	KLQQLRLTQYHGGSL HHHHHCCCHHCCCCC	22.20	21955146
58	Phosphorylation	QQLRLTQYHGGSLPN HHHCCCHHCCCCCCC	9.37	23401153
62	Phosphorylation	LTQYHGGSLPNVSQL CCHHCCCCCCCHHHH	45.29	22167270
67	Phosphorylation	GGSLPNVSQLRSSAS CCCCCCHHHHHHCHH	30.09	22617229
71	O-linked_Glycosylation	PNVSQLRSSASEFQP CCHHHHHHCHHHHCC	38.56	30059200
72	Phosphorylation	NVSQLRSSASEFQPS CHHHHHHCHHHHCCC	29.40	28555341
79	Phosphorylation	SASEFQPSFHQADNV CHHHHCCCCHHCCCC	25.28	28555341
87	Methylation	FHQADNVRGTRHHGL CHHCCCCCCCCCCCC	47.20	82797275
99	Phosphorylation	HGLVERPSRNRFHPL CCCCCCCCCCCCCCC	48.70	29449344
127	Phosphorylation	GSAFGANYSSQPLDE CCCCCCCCCCCCCCC	14.79	27642862
128	Phosphorylation	SAFGANYSSQPLDES CCCCCCCCCCCCCCC	23.46	28348404
129	Phosphorylation	AFGANYSSQPLDESW CCCCCCCCCCCCCCC	26.00	19060867
135	Phosphorylation	SSQPLDESWPRQQPP CCCCCCCCCCCCCCC	41.89	26657352
147	Sumoylation	QPPWKDEKHPGFRLT CCCCCCCCCCCCCHH	66.29	-
147	Sumoylation	QPPWKDEKHPGFRLT CCCCCCCCCCCCCHH	66.29	-
160	Phosphorylation	LTSALNRTNSDSALH HHHHHHCCCCCCCCC	37.69	21082442
162	Phosphorylation	SALNRTNSDSALHTS HHHHCCCCCCCCCHH	32.12	25159151
164	Phosphorylation	LNRTNSDSALHTSAL HHCCCCCCCCCHHHC	32.33	20873877
168	Phosphorylation	NSDSALHTSALSTKP CCCCCCCHHHCCCCC	19.28	20873877
169	Phosphorylation	SDSALHTSALSTKPQ CCCCCCHHHCCCCCC	19.23	20873877
172	Phosphorylation	ALHTSALSTKPQDPY CCCHHHCCCCCCCCC	33.82	20873877
173	Phosphorylation	LHTSALSTKPQDPYG CCHHHCCCCCCCCCC	47.82	26074081
174	Sumoylation	HTSALSTKPQDPYGG CHHHCCCCCCCCCCC	36.99	-
213	Sumoylation	ASFPGPLKEENLLNV CCCCCCCCHHHCCCC	67.14	-
222	Sumoylation	ENLLNVPKPLPKQLW HHCCCCCCCCCHHHH	55.70	-
222	Sumoylation	ENLLNVPKPLPKQLW HHCCCCCCCCCHHHH	55.70	-
226	Sumoylation	NVPKPLPKQLWETKE CCCCCCCHHHHCHHH	66.75	-
226	Sumoylation	NVPKPLPKQLWETKE CCCCCCCHHHHCHHH	66.75	-
232	Sumoylation	PKQLWETKEIQSLSG CHHHHCHHHHHHHCC	41.11	-
232	Sumoylation	PKQLWETKEIQSLSG CHHHHCHHHHHHHCC	41.11	28112733
232	Ubiquitination	PKQLWETKEIQSLSG CHHHHCHHHHHHHCC	41.11	-
236	Phosphorylation	WETKEIQSLSGRPRS HCHHHHHHHCCCCCC	30.11	28555341
238	Phosphorylation	TKEIQSLSGRPRSCD HHHHHHHCCCCCCCC	37.69	19664995
262	Phosphorylation	NGQNLGLSPFLGTLN CCCCCCCCCCCCCCC	16.29	26074081
267	Phosphorylation	GLSPFLGTLNTGGSL CCCCCCCCCCCCCCC	20.98	26074081
270	Phosphorylation	PFLGTLNTGGSLPDL CCCCCCCCCCCCCCC	46.13	26074081
273	Phosphorylation	GTLNTGGSLPDLTNL CCCCCCCCCCCCCCC	37.77	26074081
305	Phosphorylation	GSMSVGNSVNNIPAA CCCCCCCCCCCCCHH	21.94	-
320	O-linked_Glycosylation	MTHLGIRSSSGLQSS HHHHCCCCCCCCCCC	27.25	30059200
320	Phosphorylation	MTHLGIRSSSGLQSS HHHHCCCCCCCCCCC	27.25	23403867
321	O-linked_Glycosylation	THLGIRSSSGLQSSR HHHCCCCCCCCCCCC	20.69	30059200
321	Phosphorylation	THLGIRSSSGLQSSR HHHCCCCCCCCCCCC	20.69	23403867
322	Phosphorylation	HLGIRSSSGLQSSRS HHCCCCCCCCCCCCC	44.78	23403867
326	Phosphorylation	RSSSGLQSSRSNPSI CCCCCCCCCCCCCCH	32.53	23403867
327	O-linked_Glycosylation	SSSGLQSSRSNPSIQ CCCCCCCCCCCCCHH	27.11	30059200
327	Phosphorylation	SSSGLQSSRSNPSIQ CCCCCCCCCCCCCHH	27.11	23401153
329	O-linked_Glycosylation	SGLQSSRSNPSIQAT CCCCCCCCCCCHHHH	55.85	30059200
329	Phosphorylation	SGLQSSRSNPSIQAT CCCCCCCCCCCHHHH	55.85	26846344
332	Phosphorylation	QSSRSNPSIQATLNK CCCCCCCCHHHHHCH	31.42	30266825
336	Phosphorylation	SNPSIQATLNKTVLS CCCCHHHHHCHHHHH	17.94	23403867
339	Acetylation	SIQATLNKTVLSSSL CHHHHHCHHHHHHHH	43.02	26051181
340	O-linked_Glycosylation	IQATLNKTVLSSSLN HHHHHCHHHHHHHHH	26.13	30059200
340	Phosphorylation	IQATLNKTVLSSSLN HHHHHCHHHHHHHHH	26.13	27080861
343	O-linked_Glycosylation	TLNKTVLSSSLNNHP HHCHHHHHHHHHCCC	17.34	30059200
343	Phosphorylation	TLNKTVLSSSLNNHP HHCHHHHHHHHHCCC	17.34	23312004
344	Phosphorylation	LNKTVLSSSLNNHPQ HCHHHHHHHHHCCCC	34.38	23312004
345	Phosphorylation	NKTVLSSSLNNHPQT CHHHHHHHHHCCCCC	31.57	26657352
352	O-linked_Glycosylation	SLNNHPQTSVPNASA HHHCCCCCCCCCHHH	35.82	30059200
352	Phosphorylation	SLNNHPQTSVPNASA HHHCCCCCCCCCHHH	35.82	23312004
353	O-linked_Glycosylation	LNNHPQTSVPNASAL HHCCCCCCCCCHHHC	30.26	30059200
353	Phosphorylation	LNNHPQTSVPNASAL HHCCCCCCCCCHHHC	30.26	23312004
358	Phosphorylation	QTSVPNASALHPSLR CCCCCCHHHCCCCEE	37.69	28555341
363	O-linked_Glycosylation	NASALHPSLRLFSLS CHHHCCCCEEEEECC	18.51	30059200
363	Phosphorylation	NASALHPSLRLFSLS CHHHCCCCEEEEECC	18.51	24719451
368	Phosphorylation	HPSLRLFSLSNPSLS CCCEEEEECCCCCCC	35.16	30266825
370	Phosphorylation	SLRLFSLSNPSLSTT CEEEEECCCCCCCCC	45.56	28176443
373	Phosphorylation	LFSLSNPSLSTTNLS EEECCCCCCCCCCCC	38.92	30266825
375	Phosphorylation	SLSNPSLSTTNLSGP ECCCCCCCCCCCCCC	37.21	30266825
376	Phosphorylation	LSNPSLSTTNLSGPS CCCCCCCCCCCCCCC	25.62	30266825
377	Phosphorylation	SNPSLSTTNLSGPSR CCCCCCCCCCCCCCC	30.68	28176443
380	Phosphorylation	SLSTTNLSGPSRRRQ CCCCCCCCCCCCCCC	51.21	23403867
383	Phosphorylation	TTNLSGPSRRRQPPV CCCCCCCCCCCCCCC	41.78	23403867
391	Phosphorylation	RRRQPPVSPLTLSPG CCCCCCCCCCCCCCC	21.70	25463755
394	Phosphorylation	QPPVSPLTLSPGPEA CCCCCCCCCCCCHHH	28.68	21712546
396	Phosphorylation	PVSPLTLSPGPEAHQ CCCCCCCCCCHHHHC	23.68	23401153
406	Phosphorylation	PEAHQGFSRQLSSTS HHHHCCCCCCCCCCC	26.41	23403867
410	Phosphorylation	QGFSRQLSSTSPLAP CCCCCCCCCCCCCCC	24.19	23401153
411	Phosphorylation	GFSRQLSSTSPLAPY CCCCCCCCCCCCCCC	41.31	25159151
412	Phosphorylation	FSRQLSSTSPLAPYP CCCCCCCCCCCCCCC	30.87	25159151
413	Phosphorylation	SRQLSSTSPLAPYPT CCCCCCCCCCCCCCH	21.62	25159151
418	Phosphorylation	STSPLAPYPTSQMVS CCCCCCCCCHHHHCC	17.34	28464451
420	Phosphorylation	SPLAPYPTSQMVSSD CCCCCCCHHHHCCCC	26.25	22199227
421	Phosphorylation	PLAPYPTSQMVSSDR CCCCCCHHHHCCCCH	16.27	22199227
429	Phosphorylation	QMVSSDRSQLSFLPT HHCCCCHHHHCCCCC	40.23	23663014
432	Phosphorylation	SSDRSQLSFLPTEAQ CCCHHHHCCCCCHHH	19.66	19276368
436	Phosphorylation	SQLSFLPTEAQAQVS HHHCCCCCHHHHCCC	46.21	30175587
443	Phosphorylation	TEAQAQVSPPPPYPA CHHHHCCCCCCCCCC	21.43	15454081
448	Phosphorylation	QVSPPPPYPAPQELT CCCCCCCCCCCHHHC	20.14	30175587
455	Phosphorylation	YPAPQELTQPLLQQP CCCCHHHCHHHHHCC	27.64	23663014
524	Phosphorylation	VPLVQQGSRELQDSF CCCEECCCCHHHHCC	20.46	-
530	Phosphorylation	GSRELQDSFHLRPSP CCCHHHHCCCCCCCC	11.12	25627689
536	Phosphorylation	DSFHLRPSPYSNCGS HCCCCCCCCCCCCCC	30.00	25627689
539	Phosphorylation	HLRPSPYSNCGSLPN CCCCCCCCCCCCCCC	29.09	25627689
556	Phosphorylation	LPEDSSTSLFKDLNS CCCCCCCHHHHHHHH	33.48	24719451
577	Phosphorylation	EVSLNVDTPFPLEEE EEECCCCCCCCCCCC	23.65	-

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
162	S	Phosphorylation	Kinase	SIK2	Q9H0K1	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4L	Q96PU5	PMID:29505301

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
162	S	Phosphorylation	30611118
Following adenylyl cyclase activation, dephosphorylated at Ser-162 and Ser-273 resulting in its dissociation from 14-3-3 proteins probably promoting CRTC3 translocation into the nucleus.
273	S	Phosphorylation	30611118
Following adenylyl cyclase activation, dephosphorylated at Ser-162 and Ser-273 resulting in its dissociation from 14-3-3 proteins probably promoting CRTC3 translocation into the nucleus.
273	S	Phosphorylation	30611118
Phosphorylation/dephosphorylation states of Ser-273 are required for regulating transduction of CREB activity (By similarity).
391	S	Phosphorylation	18669648
May be phosphorylated at Ser-391 by MAPK3/ERK1 and/or MAPK1/ERK2 or by some cyclin-dependent kinases such as CDK1,CDK2 or CDK5.

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 CRTC3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CING_HUMAN	CGN	physical	27173435
STAT3_MOUSE	Stat3	physical	27362806
MDM2_HUMAN	MDM2	physical	27362806

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 CRTC3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-329; SER-370 ANDSER-443, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-391; SER-396 ANDSER-443, AND MASS SPECTROMETRY.	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-4, AND MASSSPECTROMETRY.	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-370 AND SER-443, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND MASSSPECTROMETRY.	17081983 [Abstract]

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