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Q96S94 (CCNL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. 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-L2
Alternative name(s):
Paneth cell-enhanced expression protein
Gene names
Name:CCNL2
ORF Names:SB138
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator which participates in regulating the pre-mRNA splicing process. Also modulates the expression of critical apoptotic factor, leading to cell apoptosis. Ref.1

Subunit structure

Interacts with CDK11A, CDK11B, CDK12, CDK13, SFRS2, SFRS7 and POLR2A, the hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II. Ref.1

Subcellular location

Nucleus speckle Ref.1.

Tissue specificity

Ubiquitously expressed, with a higher expression level observed in ovary, heart, liver and pancreas. 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 AAH71622.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAB84938.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96S94-1)

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: Q96S94-2)

Also known as: CCNL2s;

The sequence of this isoform differs from the canonical sequence as follows:
     221-226: NYMNDS → VASEGK
     227-520: Missing.
Isoform 3 (identifier: Q96S94-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-222: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 520519Cyclin-L2
PRO_0000080487

Regions

Region83 – 185103Cyclin-like 1
Region198 – 28285Cyclin-like 2
Region385 – 42339RS

Amino acid modifications

Modified residue21N-acetylalanine Ref.13 Ref.14
Modified residue3301Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue3381Phosphoserine Ref.11
Modified residue3481Phosphoserine Ref.12
Modified residue3511Phosphoserine Ref.12
Modified residue3691Phosphoserine Ref.12

Natural variations

Alternative sequence1 – 222222Missing in isoform 3.
VSP_016132
Alternative sequence221 – 2266NYMNDS → VASEGK in isoform 2.
VSP_016130
Alternative sequence227 – 520294Missing in isoform 2.
VSP_016131

Experimental info

Sequence conflict711T → S in AAH16333. Ref.6
Sequence conflict324 – 3252DG → MS in AAP97201. Ref.8
Isoform 2:
Sequence conflict2261K → IT in AAM76789. Ref.1

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: 4341E55D03D7B0E0

FASTA52058,147
        10         20         30         40         50         60 
MAAAAAAAGA AGSAAPAAAA GAPGSGGAPS GSQGVLIGDR LYSGVLITLE NCLLPDDKLR 

        70         80         90        100        110        120 
FTPSMSSGLD TDTETDLRVV GCELIQAAGI LLRLPQVAMA TGQVLFQRFF YTKSFVKHSM 

       130        140        150        160        170        180 
EHVSMACVHL ASKIEEAPRR IRDVINVFHR LRQLRDKKKP VPLLLDQDYV NLKNQIIKAE 

       190        200        210        220        230        240 
RRVLKELGFC VHVKHPHKII VMYLQVLECE RNQHLVQTSW NYMNDSLRTD VFVRFQPESI 

       250        260        270        280        290        300 
ACACIYLAAR TLEIPLPNRP HWFLLFGATE EEIQEICLKI LQLYARKKVD LTHLEGEVEK 

       310        320        330        340        350        360 
RKHAIEEAKA QARGLLPGGT QVLDGTSGFS PAPKLVESPK EGKGSKPSPL SVKNTKRRLE 

       370        380        390        400        410        420 
GAKKAKADSP VNGLPKGRES RSRSRSREQS YSRSPSRSAS PKRRKSDSGS TSGGSKSQSR 

       430        440        450        460        470        480 
SRSRSDSPPR QAPRSAPYKG SEIRGSRKSK DCKYPQKPHK SRSRSSSRSR SRSRERADNP 

       490        500        510        520 
GKYKKKSHYY RDQRRERSRS YERTGRRYER DHPGHSRHRR 

« Hide

Isoform 2 (CCNL2s) [UniParc].

Checksum: 2DA47ABC9FB2FED8
Show »

FASTA22624,621
Isoform 3 [UniParc].

Checksum: 96FA9D04F9CCB9F7
Show »

FASTA29833,839

References

« Hide 'large scale' references
[1]"Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells."
Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.
J. Biol. Chem. 279:11639-11648(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH POLR2A; CDC2L; SFRS2 AND SFRS7.
Tissue: Bone marrow.
[2]"The nucleotide sequence of a long cDNA clone isolated from human spleen."
Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Spleen.
[3]"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: Placenta and Testis.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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] (ISOFORMS 2 AND 3).
Tissue: Bone and Brain.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-226 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 367-520.
Tissue: Amygdala and Melanoma.
[8]"Cloning of a novel human cDNA homology to murine Paneth cell enhanced expression mRNA."
Zhao E.P., Yu L., Wan Y.Z., Tu Q., Zheng L.H., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 324-520.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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-330 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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-330; SER-348; SER-351 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY037150 mRNA. Translation: AAK67631.1.
AY116620 mRNA. Translation: AAM76789.1.
AK074112 mRNA. Translation: BAB84938.1. Different initiation.
AK027770 mRNA. Translation: BAG51376.1.
AK292268 mRNA. Translation: BAF84957.1.
AL391244 Genomic DNA. Translation: CAI22659.1.
AL391244, CR628411 Genomic DNA. Translation: CAI22660.2.
CR628411, AL391244 Genomic DNA. Translation: CAM12829.1.
CH471183 Genomic DNA. Translation: EAW56213.1.
CH471183 Genomic DNA. Translation: EAW56216.1.
BC016333 mRNA. Translation: AAH16333.1.
BC071622 mRNA. Translation: AAH71622.2. Different initiation.
AL834432 mRNA. Translation: CAD39092.1.
AL834441 mRNA. Translation: CAD39101.1.
AF087903 mRNA. Translation: AAP97201.1.
RefSeqNP_001034666.1. NM_001039577.3.
NP_112199.2. NM_030937.4.
UniGeneHs.515704.

3D structure databases

ProteinModelPortalQ96S94.
SMRQ96S94. Positions 52-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123566. 4 interactions.
IntActQ96S94. 1 interaction.

PTM databases

PhosphoSiteQ96S94.

Polymorphism databases

DMDM74752124.

Proteomic databases

PaxDbQ96S94.
PRIDEQ96S94.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000400809; ENSP00000383611; ENSG00000221978. [Q96S94-1]
ENST00000408918; ENSP00000386158; ENSG00000221978. [Q96S94-2]
ENST00000408952; ENSP00000386132; ENSG00000221978. [Q96S94-3]
ENST00000488340; ENSP00000424647; ENSG00000221978.
GeneID81669.
KEGGhsa:81669.
UCSCuc001aff.1. human. [Q96S94-1]
uc021oep.1. human. [Q96S94-2]

Organism-specific databases

CTD81669.
GeneCardsGC01M001321.
HGNCHGNC:20570. CCNL2.
HPAHPA053137.
MIM613482. gene.
neXtProtNX_Q96S94.
PharmGKBPA134973681.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5333.
HOVERGENHBG056044.
InParanoidQ96S94.
OMADQEYVNL.
PhylomeDBQ96S94.
TreeFamTF101011.

Enzyme and pathway databases

SignaLinkQ96S94.

Gene expression databases

ArrayExpressQ96S94.
BgeeQ96S94.
CleanExHS_CCNL2.
GenevestigatorQ96S94.

Family and domain databases

Gene3D1.10.472.10. 2 hits.
InterProIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR015429. Cyclin_C/H/T/L.
IPR017060. Cyclin_L.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERPTHR10026. PTHR10026. 1 hit.
PfamPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF036580. Cyclin_L. 1 hit.
SMARTSM00385. CYCLIN. 2 hits.
[Graphical view]
SUPFAMSSF47954. SSF47954. 2 hits.
ProtoNetSearch...

Other

ChiTaRSCCNL2. human.
GeneWikiCCNL2.
GenomeRNAi81669.
NextBio72022.
PROQ96S94.
SOURCESearch...

Entry information

Entry nameCCNL2_HUMAN
AccessionPrimary (citable) accession number: Q96S94
Secondary accession number(s): A8K8A3 expand/collapse secondary AC list , B1B152, Q5T2N5, Q5T2N6, Q6IQ12, Q7Z4Z8, Q8N3C9, Q8N3D5, Q8NHE3, Q8TEL0, Q96B00
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 108 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 1

Human chromosome 1: entries, gene names and cross-references to MIM