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Q6UUV9 (CRTC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CREB-regulated transcription coactivator 1
Alternative name(s):
Mucoepidermoid carcinoma translocated protein 1
Transducer of regulated cAMP response element-binding protein 1
Short name=TORC-1
Short name=Transducer of CREB protein 1
Gene names
Name:CRTC1
Synonyms:KIAA0616, MECT1, TORC1, WAMTP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Protein existenceEvidence 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. May be required for dendritic growth of developing cortical neurons By similarity. Ref.1 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16

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. Ref.1 Ref.11 Ref.13

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 mediated by SIKs (SIK1 and SIK2), is regulated by cAMP and calcium levels and is dependent on the phosphorylation of SIKs by LKB1 By similarity. Ref.11 Ref.13

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.

Sequence caution

The sequence AAH17075.3 differs from that shown. Reason: Erroneous initiation.

The sequence AAH23614.2 differs from that shown. Reason: Erroneous initiation.

The sequence AAP12463.1 differs from that shown. Reason: Erroneous initiation.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 634634CREB-regulated transcription coactivator 1
PRO_0000096354

Regions

Motif242 – 25817Nuclear export signal By similarity
Compositional bias299 – 36668Ser-rich

Sites

Site42 – 432Breakpoint for translocation to form the MECT1-MAML2 and MAML2-MECT1 fusion proteins Ref.2 Ref.8
Site5751Required for ubiquitination and degradation By similarity

Amino acid modifications

Modified residue1511Phosphoserine; by SIK1 and SIK2 Ref.13
Modified residue1611Phosphothreonine Ref.18

Natural variations

Alternative sequence811Q → QPSGFLGEALAAAPVSL in isoform 2.
VSP_051749
Alternative sequence475 – 50329Missing in isoform 3.
VSP_051750
Alternative sequence580 – 63455SLAGV…RMDRL → HRGHLPDGPPVSGHAGTLPL SRPDGASPARGRPCSVPRQR PSL in isoform 3.
VSP_051751
Natural variant2861T → A.
Corresponds to variant rs3746266 [ dbSNP | Ensembl ].
VAR_053934
Natural variant3111V → I. Ref.7
Corresponds to variant rs36070283 [ dbSNP | Ensembl ].
VAR_053935
Natural variant3281T → A. Ref.7
Corresponds to variant rs3746266 [ dbSNP | Ensembl ].
VAR_053936

Experimental info

Sequence conflict841F → S in BAB14822. Ref.4
Sequence conflict3841P → S in BAB14822. Ref.4
Sequence conflict5561S → G in BAB14822. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: ECDC427FF9D6920B

FASTA63467,300
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 0458940C57945F4A
Show »

FASTA65068,782
Isoform 3 [UniParc].

Checksum: B7D8709B0C731D29
Show »

FASTA59362,530

References

« Hide '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. expand/collapse author list , Zhu J., Song C., Labow M.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12147-12152(2003) [PubMed] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-151, 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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: AAH17075.3. 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.
PIRT00388.
RefSeqNP_001091952.1. NM_001098482.1.
NP_056136.2. NM_015321.2.
UniGeneHs.371096.

3D structure databases

ProteinModelPortalQ6UUV9.
SMRQ6UUV9. Positions 8-35.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116952. 6 interactions.
IntActQ6UUV9. 3 interactions.

PTM databases

PhosphoSiteQ6UUV9.

Polymorphism databases

DMDM68565585.

Proteomic databases

PaxDbQ6UUV9.
PRIDEQ6UUV9.

Protocols and materials databases

DNASU23373.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321949; ENSP00000323332; ENSG00000105662. [Q6UUV9-1]
ENST00000338797; ENSP00000345001; ENSG00000105662. [Q6UUV9-2]
GeneID23373.
KEGGhsa:23373.
UCSCuc002nkb.4. human. [Q6UUV9-1]
uc010ebv.3. human. [Q6UUV9-2]

Organism-specific databases

CTD23373.
GeneCardsGC19P018794.
HGNCHGNC:16062. CRTC1.
HPAHPA022035.
MIM607536. gene.
neXtProtNX_Q6UUV9.
PharmGKBPA30730.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG85958.
HOVERGENHBG058314.
KOK15309.
OMAMAARQAN.
OrthoDBEOG7MKW5P.
PhylomeDBQ6UUV9.
TreeFamTF321571.

Gene expression databases

ArrayExpressQ6UUV9.
BgeeQ6UUV9.
GenevestigatorQ6UUV9.

Family and domain databases

InterProIPR024786. TORC.
IPR024785. TORC_C.
IPR024784. TORC_M.
IPR024783. TORC_N.
[Graphical view]
PANTHERPTHR13589. PTHR13589. 1 hit.
PfamPF12886. TORC_C. 1 hit.
PF12885. TORC_M. 1 hit.
PF12884. TORC_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCRTC1. human.
GeneWikiCRTC1.
GenomeRNAi23373.
NextBio45456.
PROQ6UUV9.
SOURCESearch...

Entry information

Entry nameCRTC1_HUMAN
AccessionPrimary (citable) accession number: Q6UUV9
Secondary accession number(s): A6NMG5 expand/collapse secondary AC list , 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: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM