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Q52KE7 (CCNL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-L1

Short name=Cyclin-L
Alternative name(s):
Cyclin Ania-6a
Gene names
Name:Ccnl1
Synonyms:Ania6a, Ccn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length532 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Seems to be involved in the regulation of RNA polymerase II (pol II). Functions in association with cyclin-dependent kinases (CDKs). Inhibited by the CDK-specific inhibitor p21 By similarity.

Subunit structure

Interacts with POLR2A via its hyperphosphorylated C-terminal domain (CTD), CDK11A, CDK11B, CDK12, CDK13 and SFRS2. Ref.4

Subcellular location

Isoform 1: Nucleus speckle. Note: More specifically found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing. Ref.1

Isoform 2: Nucleus. Cytoplasm Ref.1.

Domain

Contains a RS region (arginine-serine dipeptide repeat) within the C-terminal domain which is the hallmark of the SR family of splicing factors. This region probably plays a role in protein-protein interactions By similarity.

Sequence similarities

Belongs to the cyclin family. Cyclin L subfamily.

Sequence caution

The sequence AAD43568.1 differs from that shown. Reason: Frameshift at positions 29 and 51.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q52KE7-1)

Also known as: Cyclin L alpha;

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.
Note: Found in the nucleus, with a speckled pattern of expression.
Isoform 2 (identifier: Q52KE7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     210-252: IIVMYLQVLE...FVRFQPETIA → VSCKVQTLQF...SFLLDVDICF
     253-532: Missing.
Note: Found both in the nucleus and cytoplasm.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 532532Cyclin-L1
PRO_0000080481

Regions

Region94 – 196103Cyclin-like 1
Region209 – 29385Cyclin-like 2
Region396 – 43843RS

Amino acid modifications

Modified residue3311Phosphothreonine By similarity
Modified residue3411Phosphoserine By similarity
Modified residue3441Phosphoserine By similarity
Modified residue3581Phosphoserine Ref.5
Modified residue3611Phosphoserine Ref.5
Modified residue4511Phosphoserine By similarity

Natural variations

Alternative sequence210 – 25243IIVMY…PETIA → VSCKVQTLQFVSIRAFSEIL NSVWRVKLTGVFKSFLLDVD ICF in isoform 2.
VSP_016126
Alternative sequence253 – 532280Missing in isoform 2.
VSP_016127

Experimental info

Sequence conflict93 – 942CE → WQ in AAL75565. Ref.1
Sequence conflict1471E → G in BAB27744. Ref.2
Sequence conflict2831E → G in BAB27744. Ref.2

Sequences

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

Last modified May 24, 2005. Version 1.
Checksum: ECBE41C070D0CA18

FASTA53260,133
        10         20         30         40         50         60 
MASGPHPTST AAAAAAAAAS ASSAAPSAGG SSSGTTTTTT TTTGGILIGD RLYSEVSLTI 

        70         80         90        100        110        120 
DHSLIPEERL SPTPSMQDGL DLPSETDLRI LGCELIQAAG ILLRLPQVAM ATGQVLFHRF 

       130        140        150        160        170        180 
FYSKSFVKHS FEIVAMACIN LASKIEEAPR RIRDVINVFH HLRQLRGKRT PSPLILDQNY 

       190        200        210        220        230        240 
INTKNQVIKA ERRVLKELGF CVHVKHPHKI IVMYLQVLEC ERNQTLVQTA WNYMNDSLRT 

       250        260        270        280        290        300 
NVFVRFQPET IACACIYLAA RALQIPLPTR PHWFLLFGTT EEEIQEICIE TLRLYTRKKP 

       310        320        330        340        350        360 
NYELLEKEVE KRKVALQEAK LKAKGLNLDG TPALSTLGGF SPASKPSSPR EVKAEEKSPV 

       370        380        390        400        410        420 
SINVKTVKKE PEDRQQASKS PYNGVRKDSK RSRTSRSASR SRSRTRSRSR SHSPRRHYNN 

       430        440        450        460        470        480 
RRSRSGTYSS RSRSRSRSHS ESPRRHHNHG SPHLKAKHTR EDLKSSNRHG HKRKKSRSRS 

       490        500        510        520        530 
QSKTRDHSDV TKKHRHERGH HRDRRERSRS FERSHKGKHH GGSRSGHGRH RR 

« Hide

Isoform 2 [UniParc].

Checksum: 9643A9CC56E56E2B
Show »

FASTA25227,441

References

« Hide 'large scale' references
[1]"Dopamine and glutamate induce distinct striatal splice forms of Ania-6, an RNA polymerase II-associated cyclin."
Berke J.D., Sgambato V., Zhu P.-P., Lavoie B., Vincent M., Krause M., Hyman S.E.
Neuron 32:277-287(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
Strain: BALB/c and C57BL/6.
Tissue: Testis.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-309 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryo and Spinal ganglion.
[3]"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).
Strain: C57BL/6.
Tissue: Eye.
[4]"CDK13/CDC2L5 interacts with L-type cyclins and regulates alternative splicing."
Chen H.H., Wong Y.H., Geneviere A.M., Fann M.J.
Biochem. Biophys. Res. Commun. 354:735-740(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK13.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF159159 mRNA. Translation: AAD43568.1. Frameshift.
AF467251 mRNA. Translation: AAL75565.1.
AK051380 mRNA. Translation: BAC34619.1.
AK011629 mRNA. Translation: BAB27744.3.
BC094383 mRNA. Translation: AAH94383.1.
CCDSCCDS17390.1. [Q52KE7-1]
RefSeqNP_064321.2. NM_019937.3. [Q52KE7-1]
UniGeneMm.175612.

3D structure databases

ProteinModelPortalQ52KE7.
SMRQ52KE7. Positions 70-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ52KE7. 1 interaction.
MINTMINT-4131139.

PTM databases

PhosphoSiteQ52KE7.

Proteomic databases

MaxQBQ52KE7.
PaxDbQ52KE7.
PRIDEQ52KE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029416; ENSMUSP00000029416; ENSMUSG00000027829. [Q52KE7-1]
GeneID56706.
KEGGmmu:56706.
UCSCuc008pku.1. mouse. [Q52KE7-1]
uc008pkx.1. mouse. [Q52KE7-2]

Organism-specific databases

CTD57018.
MGIMGI:1922664. Ccnl1.

Phylogenomic databases

eggNOGCOG5333.
GeneTreeENSGT00690000101911.
HOGENOMHOG000231292.
HOVERGENHBG056044.
InParanoidQ52KE7.
OMAFERSHKG.
OrthoDBEOG7K9K34.
PhylomeDBQ52KE7.
TreeFamTF101011.

Gene expression databases

ArrayExpressQ52KE7.
BgeeQ52KE7.
CleanExMM_CCNL1.
GenevestigatorQ52KE7.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR015429. Cyclin_C/H/T/L.
IPR017060. Cyclin_L.
IPR015431. Cyclin_L1_chr.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10026. PTHR10026. 1 hit.
PTHR10026:SF64. PTHR10026:SF64. 1 hit.
PfamPF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF036580. Cyclin_L. 1 hit.
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
ProtoNetSearch...

Other

NextBio313159.
PROQ52KE7.
SOURCESearch...

Entry information

Entry nameCCNL1_MOUSE
AccessionPrimary (citable) accession number: Q52KE7
Secondary accession number(s): Q8BQ75 expand/collapse secondary AC list , Q8R5H9, Q922K0, Q9CSZ3, Q9WV44
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 24, 2005
Last modified: July 9, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot