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Reviewed, UniProtKB/Swiss-Prot Q5RAK8 (CLOCK_PONAB)

Last modified February 9, 2010. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Circadian locomoter output cycles protein kaput
    EC=2.3.1.48
Gene names
Name: CLOCK
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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Protein attributes

Sequence length846 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

ARNTL/2-CLOCK heterodimers activate E-box element (3'-CACGTG-5') transcription of a number of proteins of the circadian clock. Activates transcription of PER1 and PER2. This transcription is inhibited in a feedback loop by PER and CRY proteins. Has intrinsic histone acetyltransferase activity and this enzymatic function contributes to chromatin-remodeling events implicated in circadian control of gene expression. Acetylates primarily histones H3 and H4. Acetylates also a non-histone substrate: ARNTL By similarity.

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Subunit structure

Component of the circadian clock oscillator which includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding requires dimerization with another bHLH protein. Heterodimerization with ARNTL is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and, for phosphorylation of both CLOCK and ARNTL. Interaction with PER and CRY proteins requires translocation to the nucleus. Interaction of the CLOCK-ARNTL heterodimer with PER or CRY inhibits transcription activation. Binds weakly ARNTL and ARNTL2 to form heterodimers which bind poorly to the E-box motif By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Shuffling between the cytoplasm and the nucleus is under circadian regulation and is ARNTL-dependent By similarity.

Post-translational modification

Phosphorylation is dependent on CLOCK-ARNTL heterodimer formation By similarity.

Sequence similarities

Contains 1 basic helix-loop-helix (bHLH) domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

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Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
Transferase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processsignal transduction

Inferred from electronic annotation. Source: InterPro

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: EC

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 846846Circadian locomoter output cycles protein kaput
PRO_0000262637

Regions

Domain48 – 8538Helix-loop-helix motif
Domain107 – 17771PAS 1
Domain262 – 33271PAS 2
Domain336 – 37944PAC
DNA binding35 – 4713Basic motif
Region514 – 56451Implicated in the circadian rhythmicity By similarity
Compositional bias483 – 828346Gln-rich

Amino acid modifications

Modified residue4081Phosphoserine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5RAK8-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: F7119E879F2C41E2

FASTA84695,354
        10         20         30         40         50         60 
MLFTVSCSKM SSIVDRDDSS IFDGLVEEDD KDKAKRVSRN KSEKKRRDQF NVLIKELGSM 

        70         80         90        100        110        120 
LPGNARKMDK STVLQKSIDF LRKHKEITAQ SDASEIRQDW KPTFLSNEEF TQLMLEALDG 

       130        140        150        160        170        180 
FFLAIMTDGS IIYVSESVTS LLEHLPSDLV DQSIFNFIPE GEHSEVYKIL STHLLESDSL 

       190        200        210        220        230        240 
TPEYLKSKNQ LEFCCHMLRG TIDPKEPSTY EYVKFIGNFK SLNSVSSSAH NGFEGTIQRT 

       250        260        270        280        290        300 
HRPSYEDRVC FVATVRLATP QFIKEMCTVE EPNEEFASRH SLEWKFLFLD HRAPPIIGYL 

       310        320        330        340        350        360 
PFEVLGTSGY DYYHVDDLEN LAKCHEHLMQ YGKGKSCYYR FLTKGQQWIW LQTHYYITYH 

       370        380        390        400        410        420 
QWNSRPEFIV CTHTVVSYAE VRAERRRELS IEESLPEIAA DKSQDSGSDN RINTVSLKEA 

       430        440        450        460        470        480 
LERFDHSPTP SASSRSSRKS SHTAVSDPSS TPTKIPTDTS TPPRQHLPAH EKMVQRRSSF 

       490        500        510        520        530        540 
SSQSINSQSV GSSLTQPVMS QATNLPIPQG MSQFQFSAQL GAMQHLKDQL EQRTRMIEAN 

       550        560        570        580        590        600 
IHRQQEELRK IQEQLQMVHG QGLQMFLQQP NPGLNFGSVQ LSSGNSSNIQ QLAPINMQGQ 

       610        620        630        640        650        660 
VVPTNQIQSG MNTGHIGTTQ HMIQQQTLQS TSTQSQQNVL SGHSQQTSLP SQTQSTLTAP 

       670        680        690        700        710        720 
LYNTMVISQP AAGSMVQIPS SMPQNSTQSA AVTTFTQDRQ IRFSQGQQLV TKLVTAPVAC 

       730        740        750        760        770        780 
GAVMVPSTML MGQVVTAYPT FATQQQQSQT LSVTQQRQQQ SSQEQQLTSV QQPSQAQLTQ 

       790        800        810        820        830        840 
PPQQFLQTSR LLHGNPSTQL ILSAAFPLQQ STFPQSHHQQ HQSQQQQQLS RHRTDSLPDP 


SKVQPQ

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR859007 mRNA. Translation: CAH91202.1.
RefSeqNP_001125706.1.
UniGenePab.7567

3D structure databases

HSSPHSSP built from PDB template 1AM9 based on UniProtKB P36956.
SMRQ5RAK8. Positions 32-86, 119-380.
ModBaseSearch...

Genome annotation databases

GeneID100172630.

Organism-specific databases

CTD100172630.

Phylogenomic databases

HOVERGENQ5RAK8.
InParanoidQ5RAK8.

Enzyme and pathway databases

BRENDA2.3.1.48. 269192.

Family and domain databases

InterProIPR001092. HLH_DNA-bd_dom.
IPR011598. HLH_DNA_bd.
IPR001067. Nuc_translocat.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR013655. PAS_fold_3.
[Graphical view]
Gene3DG3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.
PfamPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
PF08447. PAS_3. 1 hit.
[Graphical view]
PRINTSPR00785. NCTRNSLOCATR.
SMARTSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
PROSITEPS50888. HLH. 1 hit.
PS50113. PAC. False negative.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCLOCK_PONAB
AccessionPrimary (citable) accession number: Q5RAK8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 21, 2004
Last modified: February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents