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Q9UK58 (CCNL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:CCNL1
ORF Names:BM-001, UNQ530/PRO1073
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length526 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) and has a role in the second step of splicing. May be a candidate proto-oncogene in head and neck squamous cell carcinomas (HNSCC). Inhibited by the CDK-specific inhibitor p21. Ref.1 Ref.7 Ref.8

Subunit structure

Interacts with POLR2A via its hyperphosphorylated C-terminal domain (CTD) By similarity. Interacts with CDK11A, CDK11B, CDK12, CDK13 and SFRS2. Ref.1

Subcellular location

Nucleus speckle By similarity. 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 By similarity.

Tissue specificity

Ubiquitous with higher level in thymus. Overexpression in primary tumors of head and neck squamous cell carcinomas (HNSCC). Ref.1 Ref.7 Ref.8

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. Ref.1

Miscellaneous

CCNL1 is amplified in several HNSCC. May play a critical role in the formation of loco-regional metastases and an unfavorable clinical outcome of HNSCC.

Sequence similarities

Belongs to the cyclin family. Cyclin L subfamily.

Sequence caution

The sequence AAF64257.1 differs from that shown. Reason: Probable cloning artifact.

The sequence AAQ89026.1 differs from that shown. Reason: Probable cloning artifact.

Alternative products

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

Note: Ccnl1 is an immediate-early gene with independently regulated isoforms.
Isoform 1 (identifier: Q9UK58-1)

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.
Isoform 2 (identifier: Q9UK58-4)

Also known as: Cyclin L beta;

The sequence of this isoform differs from the canonical sequence as follows:
     226-232: NYMNDSL → VVHDGKS
     233-526: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 3 (identifier: Q9UK58-5)

Also known as: Cyclin L gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     163-172: RTPSPLILDQ → SDQLHLPKPG
     173-526: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Cyclin-L1
PRO_0000080480

Regions

Region88 – 190103Cyclin-like 1
Region203 – 28785Cyclin-like 2
Region390 – 43243RS

Amino acid modifications

Modified residue3251Phosphothreonine Ref.10
Modified residue3351Phosphoserine Ref.10 Ref.12 Ref.13
Modified residue3381Phosphoserine Ref.10 Ref.12
Modified residue3521Phosphoserine Ref.12 Ref.13 Ref.14
Modified residue3551Phosphoserine By similarity
Modified residue4451Phosphoserine Ref.13

Natural variations

Alternative sequence163 – 17210RTPSPLILDQ → SDQLHLPKPG in isoform 3.
VSP_016120
Alternative sequence173 – 526354Missing in isoform 3.
VSP_016121
Alternative sequence226 – 2327NYMNDSL → VVHDGKS in isoform 2.
VSP_016122
Alternative sequence233 – 526294Missing in isoform 2.
VSP_016123

Experimental info

Sequence conflict1491V → L in AAH67812. Ref.4
Sequence conflict507 – 5082RS → SP in AAF64257. Ref.5

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 64C0CAEF54A3E9F9

FASTA52659,634
        10         20         30         40         50         60 
MASGPHSTAT AAAAASSAAP SAGGSSSGTT TTTTTTTGGI LIGDRLYSEV SLTIDHSLIP 

        70         80         90        100        110        120 
EERLSPTPSM QDGLDLPSET DLRILGCELI QAAGILLRLP QVAMATGQVL FHRFFYSKSF 

       130        140        150        160        170        180 
VKHSFEIVAM ACINLASKIE EAPRRIRDVI NVFHHLRQLR GKRTPSPLIL DQNYINTKNQ 

       190        200        210        220        230        240 
VIKAERRVLK ELGFCVHVKH PHKIIVMYLQ VLECERNQTL VQTAWNYMND SLRTNVFVRF 

       250        260        270        280        290        300 
QPETIACACI YLAARALQIP LPTRPHWFLL FGTTEEEIQE ICIETLRLYT RKKPNYELLE 

       310        320        330        340        350        360 
KEVEKRKVAL QEAKLKAKGL NPDGTPALST LGGFSPASKP SSPREVKAEE KSPISINVKT 

       370        380        390        400        410        420 
VKKEPEDRQQ ASKSPYNGVR KDSKRSRNSR SASRSRSRTR SRSRSHTPRR HYNNRRSRSG 

       430        440        450        460        470        480 
TYSSRSRSRS RSHSESPRRH HNHGSPHLKA KHTRDDLKSS NRHGHKRKKS RSRSQSKSRD 

       490        500        510        520 
HSDAAKKHRH ERGHHRDRRE RSRSFERSHK SKHHGGSRSG HGRHRR 

« Hide

Isoform 2 (Cyclin L beta) [UniParc].

Checksum: ACD35FB41FF67306
Show »

FASTA23225,408
Isoform 3 (Cyclin L gamma) [UniParc].

Checksum: 972B0E52D25720E1
Show »

FASTA17218,322

References

« Hide 'large scale' references
[1]"Cyclin L is an RS domain protein involved in pre-mRNA splicing."
Dickinson L.A., Edgar A.J., Ehley J., Gottesfeld J.M.
J. Biol. Chem. 277:25465-25473(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE SPECIFICITY, DOMAIN, INTERACTION WITH CDC2L AND SFRS2.
Tissue: Lung.
[2]"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 1).
[3]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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).
Tissue: Brain and Testis.
[5]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-526 (ISOFORM 1).
Tissue: Bone marrow.
[6]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 226-526 (ISOFORM 1).
[7]"Amplicon mapping and transcriptional analysis pinpoint cyclin L as a candidate oncogene in head and neck cancer."
Redon R., Hussenet T., Bour G., Caulee K., Jost B., Muller D., Abecassis J., du Manoir S.
Cancer Res. 62:6211-6217(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[8]"Amplification of Cyclin L1 is associated with lymph node metastases in head and neck squamous cell carcinoma (HNSCC)."
Sticht C., Hofele C., Flechtenmacher C., Bosch F.X., Freier K., Lichter P., Joos S.
Br. J. Cancer 92:770-774(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-325; SER-335 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-338 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-352 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF180920 mRNA. Translation: AAD53184.1.
AK022974 mRNA. Translation: BAG51145.1.
AF367476 mRNA. Translation: AAM21204.1.
AF367477 mRNA. Translation: AAM21205.1.
AY034790 mRNA. Translation: AAK61551.1.
CH471052 Genomic DNA. Translation: EAW78712.1.
BC007081 mRNA. Translation: AAH07081.1.
BC038394 mRNA. Translation: AAH38394.1.
BC067812 mRNA. Translation: AAH67812.1.
AF208843 mRNA. Translation: AAF64257.1. Sequence problems.
AY358663 mRNA. Translation: AAQ89026.1. Sequence problems.
RefSeqNP_064703.1. NM_020307.2.
XP_005247707.1. XM_005247650.1.
XP_005247708.1. XM_005247651.1.
UniGeneHs.4859.

3D structure databases

ProteinModelPortalQ9UK58.
SMRQ9UK58. Positions 64-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121327. 5 interactions.
IntActQ9UK58. 8 interactions.
MINTMINT-4541433.
STRING9606.ENSP00000295926.

PTM databases

PhosphoSiteQ9UK58.

Polymorphism databases

DMDM74753368.

Proteomic databases

PaxDbQ9UK58.
PRIDEQ9UK58.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295925; ENSP00000295925; ENSG00000163660. [Q9UK58-5]
ENST00000295926; ENSP00000295926; ENSG00000163660. [Q9UK58-1]
ENST00000465947; ENSP00000418094; ENSG00000163660. [Q9UK58-5]
ENST00000470121; ENSP00000417237; ENSG00000163660. [Q9UK58-4]
ENST00000475298; ENSP00000417343; ENSG00000163660. [Q9UK58-5]
ENST00000477127; ENSP00000418449; ENSG00000163660. [Q9UK58-5]
GeneID57018.
KEGGhsa:57018.
UCSCuc003fbe.3. human. [Q9UK58-1]

Organism-specific databases

CTD57018.
GeneCardsGC03M156864.
HGNCHGNC:20569. CCNL1.
HPAHPA034752.
MIM613384. gene.
neXtProtNX_Q9UK58.
PharmGKBPA134980948.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5333.
HOVERGENHBG056044.
InParanoidQ9UK58.
OMAFERSHKG.
PhylomeDBQ9UK58.
TreeFamTF101011.

Enzyme and pathway databases

SignaLinkQ9UK58.

Gene expression databases

ArrayExpressQ9UK58.
BgeeQ9UK58.
CleanExHS_CCNL1.
GenevestigatorQ9UK58.

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_met.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10026. PTHR10026. 1 hit.
PTHR10026:SF2. PTHR10026:SF2. 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

GeneWikiCCNL1.
GenomeRNAi57018.
NextBio62766.
PROQ9UK58.
SOURCESearch...

Entry information

Entry nameCCNL1_HUMAN
AccessionPrimary (citable) accession number: Q9UK58
Secondary accession number(s): B3KMY3 expand/collapse secondary AC list , Q6NVY9, Q6UWS7, Q8NI48, Q96QT0, Q9NZF3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 116 of the entry and version 1 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 chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM