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Protein

Cyclin-L2

Gene

Ccnl2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in pre-mRNA splicing. May induce cell death, possibly by acting on the transcription and RNA processing of apoptosis-related factors.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-L2
Gene namesi
Name:Ccnl2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1309149. Ccnl2.

Subcellular locationi

  • Nucleus speckle By similarity
  • Nucleusnucleoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Cyclin-L2PRO_0000080489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei330 – 3301PhosphoserineBy similarity
Modified residuei337 – 3371PhosphoserineBy similarity
Modified residuei347 – 3471PhosphoserineBy similarity
Modified residuei350 – 3501PhosphoserineBy similarity
Modified residuei368 – 3681PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5I0H5.
PRIDEiQ5I0H5.

PTM databases

iPTMnetiQ5I0H5.

Expressioni

Gene expression databases

ExpressionAtlasiQ5I0H5. baseline and differential.

Interactioni

Subunit structurei

Interacts with CDK11A, CDK11B, CDK12, CDK13 and POLR2A, the hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II. May form a ternary complex with CDK11B and casein kinase II (CKII). Interacts with pre-mRNA-splicing factors, including at least SRSF1, SRSF2 AND SRSF7/SLU7.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025531.

Structurei

3D structure databases

ProteinModelPortaliQ5I0H5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 183103Cyclin-like 1Add
BLAST
Regioni196 – 28085Cyclin-like 2Add
BLAST
Regioni384 – 42239RSAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the cyclin family. Cyclin L subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0835. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000231292.
HOVERGENiHBG056044.
InParanoidiQ5I0H5.
OMAiYRKSKDC.
OrthoDBiEOG7K9K34.
PhylomeDBiQ5I0H5.
TreeFamiTF101011.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR015429. Cyclin_L/T.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036580. Cyclin_L. 1 hit.
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5I0H5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAAAAGASG LMAPALAACS SGSGGAAPGS QGVLIGDRLY SGVLITLENC
60 70 80 90 100
LLPDDKLRFT PSMSSGLDID TETGLRVVGC ELIQAAGILL RLPQVAMATG
110 120 130 140 150
QVLFQRFFYT KSFVKHSMEH VSMACVHLAS KIEEAPRRIR DVINVFHRLR
160 170 180 190 200
HLREKKKPVP LVLDQEYVNL KNQIIKAERR VLKELGFCVH VKHPHKIIVM
210 220 230 240 250
YLQVLECERN QHLVQTAWNY MNDSLRTDVF VRFQPESIAC ACIYLAARTL
260 270 280 290 300
EIPLPNRPHW FLLFGATEEE IQEICFKILQ LYTRKKVDLT HLESEVEKRK
310 320 330 340 350
HAIEEAKARA KGLLPPGSAP GLDSATAGFS PAPKPESPKE GKGSKSSPLS
360 370 380 390 400
VKNAKRKMEG PKKAKGDSPV NGLLKGQESR SQSRSREQSY SRSPSRSASP
410 420 430 440 450
KRRKSDSGST SGGSKSQSRS RSRSDSPPRQ VHRGAPYKGS EVRGSRKSKD
460 470 480 490 500
CKHLTQKPHK SRSRSSSRSR SRSRERTDSS GKYKKKSHYY RDQRRERSRS
510 520
YERTGHRYER DHPGHSRHRR
Length:520
Mass (Da):58,246
Last modified:November 8, 2005 - v2
Checksum:iCF78FB24BE3EFA7C
GO
Isoform 2 (identifier: Q5I0H5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     219-224: NYMNDS → VASEGK
     225-520: Missing.

Show »
Length:224
Mass (Da):24,620
Checksum:iEEB2D3920BF2C54C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei219 – 2246NYMNDS → VASEGK in isoform 2. 1 PublicationVSP_016136
Alternative sequencei225 – 520296Missing in isoform 2. 1 PublicationVSP_016137Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03040241 Genomic DNA. No translation available.
BC088316 mRNA. Translation: AAH88316.1.
RefSeqiNP_001013112.1. NM_001013094.1. [Q5I0H5-2]
XP_006239607.1. XM_006239545.2. [Q5I0H5-1]
UniGeneiRn.232195.
Rn.43669.

Genome annotation databases

EnsembliENSRNOT00000089936; ENSRNOP00000068952; ENSRNOG00000018691. [Q5I0H5-2]
GeneIDi298686.
KEGGirno:298686.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03040241 Genomic DNA. No translation available.
BC088316 mRNA. Translation: AAH88316.1.
RefSeqiNP_001013112.1. NM_001013094.1. [Q5I0H5-2]
XP_006239607.1. XM_006239545.2. [Q5I0H5-1]
UniGeneiRn.232195.
Rn.43669.

3D structure databases

ProteinModelPortaliQ5I0H5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025531.

PTM databases

iPTMnetiQ5I0H5.

Proteomic databases

PaxDbiQ5I0H5.
PRIDEiQ5I0H5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000089936; ENSRNOP00000068952; ENSRNOG00000018691. [Q5I0H5-2]
GeneIDi298686.
KEGGirno:298686.

Organism-specific databases

CTDi81669.
RGDi1309149. Ccnl2.

Phylogenomic databases

eggNOGiKOG0835. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00760000119191.
HOGENOMiHOG000231292.
HOVERGENiHBG056044.
InParanoidiQ5I0H5.
OMAiYRKSKDC.
OrthoDBiEOG7K9K34.
PhylomeDBiQ5I0H5.
TreeFamiTF101011.

Miscellaneous databases

PROiQ5I0H5.

Gene expression databases

ExpressionAtlasiQ5I0H5. baseline and differential.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR004367. Cyclin_C-dom.
IPR015429. Cyclin_L/T.
IPR006671. Cyclin_N.
[Graphical view]
PfamiPF02984. Cyclin_C. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFiPIRSF036580. Cyclin_L. 1 hit.
SMARTiSM00385. CYCLIN. 2 hits.
SM01332. Cyclin_C. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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 2).
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCCNL2_RAT
AccessioniPrimary (citable) accession number: Q5I0H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: June 8, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.