Reviewed, UniProtKB/Swiss-Prot Q6UUV9 (CRTC1_HUMAN)

Names and origin

Protein names

Recommended name:
    CREB-regulated transcription coactivator 1
Alternative name(s):
    Transducer of regulated cAMP response element-binding protein 1
      Short name=TORC-1
      Short name=Transducer of CREB protein 1
    Mucoepidermoid carcinoma translocated protein 1

Gene names

Name:	CRTC1
Synonyms:	KIAA0616, MECT1, TORC1, WAMTP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	634 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR). In the hippocampus, involved in late-phase long-term potentiation (L-LTP) maintenance at the Schaffer collateral-CA1 synapses By similarity. Ref.10 Ref.1
Subunit structure	Binds, as a tetramer, through its N-terminal region, with the bZIP domain of CREB1. 'Arg-314' in the bZIP domain of CREB1 is essential for this interaction. Interaction, via its C-terminal, with TAF4, enhances recruitment of TAF4 to CREB1. Binds HTLV1 Tax. Ref.10
Subcellular location	Cytoplasm. Nucleus. Note: 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 levels.
Tissue specificity	Highly expressed in adult and fetal brain. Located to specific regions such as the prefrontal cortex and cerebellum. Very low expression in other tissues such as heart, spleen, lung, skeletal muscle, salivary gland, ovary and kidney. Ref.8 Ref.15
Post-translational modification	Phosphorylation/dephosphorylation states of Ser-151 are required for regulating transduction of CREB activity. TORCs are inactive when phosphorylated, and active when dephosphorylated at this site. This primary site of phosphorylation, is regulated by cAMP and calcium levels and is dependent on the phosphorylation of SIKs by LKB1 By similarity. Phosphorylated upon DNA damage, probably by ATM or ATR.
Involvement in disease	A chromosomal aberration involving CRTC1 is found in mucoepidermoid carcinomas, benign Warthin tumors and clear cell hidradenomas. Translocation t(11;19)(q21;p13) with MAML2. The fusion protein consists of the N-terminus of CRTC1 joined to the C-terminus of MAML2. The reciprocal fusion protein consisting of the N-terminus of MAML2 joined to the C-terminus of CRTC1 has been detected in a small number of mucoepidermoid carcinomas.
Sequence similarities	Belongs to the TORC family.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Molecular function	Activator
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of transcription from RNA polymerase II promoter Ref.10 Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	cAMP response element binding protein binding Ref.10 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: Q6UUV9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q6UUV9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     81-81: Q → QPSGFLGEALAAAPVSL

Note: No experimental confirmation available.

Isoform 3 Ref.2 (identifier: Q6UUV9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     475-503: Missing.
     580-634: SLAGVGDVSF...TEDTFRMDRL → HRGHLPDGPP...CSVPRQRPSL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 634	634	CREB-regulated transcription coactivator 1		PRO_0000096354
Regions
	Motif	242 – 258	17	Nuclear export signal By similarity
	Compositional bias	299 – 366	68	Ser-rich
Sites
	Site	42 – 43	2	Breakpoint for translocation to form the MECT1-MAML2 and MAML2-MECT1 fusion proteins Ref.8 Ref.2
	Site	575	1	Required for ubiquitination and degradation By similarity
Amino acid modifications
	Modified residue	64	1	Phosphoserine By similarity
	Modified residue	86	1	Phosphoserine By similarity
	Modified residue	139	1	Phosphoserine By similarity
	Modified residue	149	1	Phosphothreonine By similarity
	Modified residue	151	1	Phosphoserine; by SNF1lK2 Ref.17 Ref.18
	Modified residue	161	1	Phosphothreonine Ref.18
	Modified residue	172	1	Phosphoserine Ref.17
	Modified residue	277	1	Phosphoserine By similarity
	Modified residue	440	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	81	1	Q → QPSGFLGEALAAAPVSL in isoform 2.		VSP_051749
	Alternative sequence	475 – 503	29	Missing in isoform 3.		VSP_051750
	Alternative sequence	580 – 634	55	SLAGV…RMDRL → HRGHLPDGPPVSGHAGTLPL SRPDGASPARGRPCSVPRQR PSL in isoform 3.		VSP_051751
	Natural variant	286	1	T → A: dbSNP rs3746266.		VAR_053934
	Natural variant	311	1	V → I: dbSNP rs36070283. Ref.7		VAR_053935
	Natural variant	328	1	T → A: dbSNP rs3746266. Ref.7		VAR_053936
Experimental info
	Sequence conflict	84	1	F → S in BAB14822. Ref.4
	Sequence conflict	384	1	P → S in BAB14822. Ref.4
	Sequence conflict	556	1	S → G in BAB14822. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: ECDC427FF9D6920B	FASTA	634	67,300
	10 20 30 40 50 60 MATSNNPRKF SEKIALHNQK QAEETAAFEE VMKDLSLTRA ARLQLQKSQY LQLGPSRGQY 70 80 90 100 110 120 YGGSLPNVNQ IGSGTMDLPF QTPFQSSGLD TSRTTRHHGL VDRVYRERGR LGSPHRRPLS 130 140 150 160 170 180 VDKHGRQADS CPYGTMYLSP PADTSWRRTN SDSALHQSTM TPTQPESFSS GSQDVHQKRV 190 200 210 220 230 240 LLLTVPGMEE TTSEADKNLS KQAWDTKKTG SRPKSCEVPG INIFPSADQE NTTALIPATH 250 260 270 280 290 300 NTGGSLPDLT NIHFPSPLPT PLDPEEPTFP ALSSSSSTGN LAANLTHLGI GGAGQGMSTP 310 320 330 340 350 360 GSSPQHRPAG VSPLSLSTEA RRQQASPTLS PLSPITQAVA MDALSLEQQL PYAFFTQAGS 370 380 390 400 410 420 QQPPPQPQPP PPPPPASQQP PPPPPPQAPV RLPPGGPLLP SASLTRGPQP PPLAVTVPSS 430 440 450 460 470 480 LPQSPPENPG QPSMGIDIAS APALQQYRTS AGSPANQSPT SPVSNQGFSP GSSPQHTSTL 490 500 510 520 530 540 GSVFGDAYYE QQMAARQANA LSHQLEQFNM MENAISSSSL YSPGSTLNYS QAAMMGLTGS 550 560 570 580 590 600 HGSLPDSQQL GYASHSGIPN IILTVTGESP PSLSKELTSS LAGVGDVSFD SDSQFPLDEL 610 620 630 KIDPLTLDGL HMLNDPDMVL ADPATEDTFR MDRL
	Isoform 2. Checksum: 0458940C57945F4A	FASTA	650	68,782
	10 20 30 40 50 60 MATSNNPRKF SEKIALHNQK QAEETAAFEE VMKDLSLTRA ARLQLQKSQY LQLGPSRGQY 70 80 90 100 110 120 YGGSLPNVNQ IGSGTMDLPF QPSGFLGEAL AAAPVSLTPF QSSGLDTSRT TRHHGLVDRV 130 140 150 160 170 180 YRERGRLGSP HRRPLSVDKH GRQADSCPYG TMYLSPPADT SWRRTNSDSA LHQSTMTPTQ 190 200 210 220 230 240 PESFSSGSQD VHQKRVLLLT VPGMEETTSE ADKNLSKQAW DTKKTGSRPK SCEVPGINIF 250 260 270 280 290 300 PSADQENTTA LIPATHNTGG SLPDLTNIHF PSPLPTPLDP EEPTFPALSS SSSTGNLAAN 310 320 330 340 350 360 LTHLGIGGAG QGMSTPGSSP QHRPAGVSPL SLSTEARRQQ ASPTLSPLSP ITQAVAMDAL 370 380 390 400 410 420 SLEQQLPYAF FTQAGSQQPP PQPQPPPPPP PASQQPPPPP PPQAPVRLPP GGPLLPSASL 430 440 450 460 470 480 TRGPQPPPLA VTVPSSLPQS PPENPGQPSM GIDIASAPAL QQYRTSAGSP ANQSPTSPVS 490 500 510 520 530 540 NQGFSPGSSP QHTSTLGSVF GDAYYEQQMA ARQANALSHQ LEQFNMMENA ISSSSLYSPG 550 560 570 580 590 600 STLNYSQAAM MGLTGSHGSL PDSQQLGYAS HSGIPNIILT VTGESPPSLS KELTSSLAGV 610 620 630 640 650 GDVSFDSDSQ FPLDELKIDP LTLDGLHMLN DPDMVLADPA TEDTFRMDRL
	Isoform 3. Checksum: B7D8709B0C731D29	FASTA	593	62,530
	10 20 30 40 50 60 MATSNNPRKF SEKIALHNQK QAEETAAFEE VMKDLSLTRA ARLQLQKSQY LQLGPSRGQY 70 80 90 100 110 120 YGGSLPNVNQ IGSGTMDLPF QTPFQSSGLD TSRTTRHHGL VDRVYRERGR LGSPHRRPLS 130 140 150 160 170 180 VDKHGRQADS CPYGTMYLSP PADTSWRRTN SDSALHQSTM TPTQPESFSS GSQDVHQKRV 190 200 210 220 230 240 LLLTVPGMEE TTSEADKNLS KQAWDTKKTG SRPKSCEVPG INIFPSADQE NTTALIPATH 250 260 270 280 290 300 NTGGSLPDLT NIHFPSPLPT PLDPEEPTFP ALSSSSSTGN LAANLTHLGI GGAGQGMSTP 310 320 330 340 350 360 GSSPQHRPAG VSPLSLSTEA RRQQASPTLS PLSPITQAVA MDALSLEQQL PYAFFTQAGS 370 380 390 400 410 420 QQPPPQPQPP PPPPPASQQP PPPPPPQAPV RLPPGGPLLP SASLTRGPQP PPLAVTVPSS 430 440 450 460 470 480 LPQSPPENPG QPSMGIDIAS APALQQYRTS AGSPANQSPT SPVSNQGFSP GSSPQLEQFN 490 500 510 520 530 540 MMENAISSSS LYSPGSTLNY SQAAMMGLTG SHGSLPDSQQ LGYASHSGIP NIILTVTGES 550 560 570 580 590 PPSLSKELTS HRGHLPDGPP VSGHAGTLPL SRPDGASPAR GRPCSVPRQR PSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a family of cAMP response element-binding protein coactivators by genome-scale functional analysis in mammalian cells." Iourgenko V., Zhang W., Mickanin C., Daly I., Jiang C., Hexham J.M., Orth A.P., Miraglia L., Meltzer J., Garza D., Chirn G.-W., McWhinnie E., Cohen D., Skelton J., Terry R., Yu Y., Bodian D., Buxton F.P. , Zhu J., Song C., Labow M.A. Proc. Natl. Acad. Sci. U.S.A. 100:12147-12152(2003) [PubMed: 14506290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CREB1.
[2]	"t(11;19)(q21;p13) translocation in mucoepidermoid carcinoma creates a novel fusion product that disrupts a Notch signaling pathway." Tonon G., Modi S., Wu L., Kubo A., Coxon A.B., Komiya T., O'Neil K., Stover K., El-Naggar A., Griffin J.D., Kirsch I.R., Kaye F.J. Nat. Genet. 33:208-213(2003) [PubMed: 12539049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHROMOSOMAL TRANSLOCATION WITH MAML2.
[3]	Erratum Tonon G., Modi S., Wu L., Kubo A., Coxon A.B., Komiya T., O'Neil K., Stover K., El-Naggar A., Griffin J.D., Kirsch I.R., Kaye F.J. Nat. Genet. 33:408-408(2003)
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Embryo.
[5]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-311 AND ALA-328. Tissue: Brain, Colon and Eye.
[8]	"Altered Notch signaling resulting from expression of a WAMTP1-MAML2 gene fusion in mucoepidermoid carcinomas and benign Warthin's tumors." Enlund F., Behboudi A., Andren Y., Oberg C., Lendahl U., Mark J., Stenman G. Exp. Cell Res. 292:21-28(2004) [PubMed: 14720503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-104 (ISOFORMS 1/3), TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH MAML2. Tissue: Carcinoma.
[9]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed: 9734811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-634 (ISOFORM 2). Tissue: Brain.
[10]	"TORCs: transducers of regulated CREB activity." Conkright M.D., Canettieri G., Screaton R., Guzman E., Miraglia L., Hogenesch J.B., Montminy M. Mol. Cell 12:413-423(2003) [PubMed: 14536081] [Abstract] Cited for: FUNCTION, SUBUNIT, INTERACTION WITH CREB1 AND TAF4.
[11]	"Activation of cAMP response element-mediated gene expression by regulated nuclear transport of TORC proteins." Bittinger M.A., McWhinnie E., Meltzer J., Iourgenko V., Latario B., Liu X., Chen C.H., Song C., Garza D., Labow M. Curr. Biol. 14:2156-2161(2004) [PubMed: 15589160] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[12]	"Clear cell hidradenoma of the skin-a third tumor type with a t(11;19)-associated TORC1-MAML2 gene fusion." Behboudi A., Winnes M., Gorunova L., van den Oord J.J., Mertens F., Enlund F., Stenman G. Genes Chromosomes Cancer 43:202-205(2005) [PubMed: 15729701] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION.
[13]	"Silencing the constitutive active transcription factor CREB by the LKB1-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) [PubMed: 16817901] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[14]	"TORC1 and TORC2 coactivators are required for tax activation of the human T-cell leukemia virus type 1 long terminal repeats." Siu Y.-T., Chin K.-T., Siu K.-L., Yee Wai Choy E., Jeang K.-T., Jin D.-Y. J. Virol. 80:7052-7059(2006) [PubMed: 16809310] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX, FUNCTION.
[15]	"Transducer of regulated CREB-binding proteins (TORCs) induce PGC-1alpha transcription and mitochondrial biogenesis in muscle cells." Wu Z., Huang X., Feng Y., Handschin C., Feng Y., Gullicksen P.S., Bare O., Labow M., Spiegelman B., Stevenson S.C. Proc. Natl. Acad. Sci. U.S.A. 103:14379-14384(2006) [PubMed: 16980408] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[16]	"Dephosphorylation of TORC initiates expression of the StAR gene." Takemori H., Kanematsu M., Kajimura J., Hatano O., Katoh Y., Lin X.-Z., Min L., Yamazaki T., Doi J., Okamoto M. Mol. Cell. Endocrinol. 265:196-204(2007) [PubMed: 17210223] [Abstract] Cited for: FUNCTION.
[17]	"ATM and ATR substrate analysis reveals extensive protein networks responsive 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) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND SER-172, MASS SPECTROMETRY.
[18]	"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) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND THR-161, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY360171 mRNA. Translation: AAQ98856.1. AY040323 mRNA. Translation: AAK93832.1. AY040324 mRNA. Translation: AAK93833.1. Different termination. AK024089 mRNA. Translation: BAB14822.1. AC003107 Genomic DNA. No translation available. AC004476 Genomic DNA. No translation available. AC006123 Genomic DNA. Translation: AAC97072.1. CH471106 Genomic DNA. Translation: EAW84730.1. BC017075 mRNA. Translation: AAH17075.2. Different initiation. BC023614 mRNA. Translation: AAH23614.2. Different initiation. BC028050 mRNA. Translation: AAH28050.1. AB014516 mRNA. Translation: BAA31591.1. AY186997 mRNA. Translation: AAP12462.1. Different termination. AY186998 mRNA. Translation: AAP12463.1. Different initiation.
IPI	IPI00303383. IPI00412329. IPI00783099.
PIR	T00388.
RefSeq	NP_001091952.1. NP_056136.2.
UniGene	Hs.371096 Hs.428214
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q6UUV9.
Proteomic databases
PRIDE	Q6UUV9.
Genome annotation databases
Ensembl	ENSG00000105662. Homo sapiens. [Contig view]
GeneID	23373.
KEGG	hsa:23373.
Organism-specific databases
GeneCards	GC19P018656.
H-InvDB	HIX0014922. HIX0057218.
HGNC	HGNC:16062. CRTC1.
MIM	607536. gene.
PharmGKB	PA30730.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q6UUV9.
OMA	Q6UUV9. VFGDSYY.
Gene expression databases
ArrayExpress	Q6UUV9.
Bgee	Q6UUV9.
GermOnline	ENSG00000105662. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	45456.
SOURCE	Search...

Entry information

Entry name

CRTC1_HUMAN

Accession

Primary (citable) accession number: Q6UUV9
Secondary accession number(s): A6NMG5 , O75114, Q6Y3A3, Q7LDZ2, Q8IUL3, Q8IZ34, Q8IZL1, Q8N6W3, Q96AI8, Q9H801

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)