CCNL2_RAT
ID CCNL2_RAT Reviewed; 520 AA.
AC Q5I0H5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cyclin-L2;
GN Name=Ccnl2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in pre-mRNA splicing. May induce cell death,
CC possibly by acting on the transcription and RNA processing of
CC apoptosis-related factors. {ECO:0000250|UniProtKB:Q96S94}.
CC -!- SUBUNIT: Interacts with CDK11A, CDK11B, CDK12, CDK13 and POLR2A, the
CC hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II. May
CC form a ternary complex with CDK11B and casein kinase II (CKII).
CC Interacts with pre-mRNA-splicing factors, including at least SRSF1,
CC SRSF2 AND SRSF7/SLU7. {ECO:0000250|UniProtKB:Q96S94,
CC ECO:0000250|UniProtKB:Q9JJA7}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q96S94}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96S94}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5I0H5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5I0H5-2; Sequence=VSP_016136, VSP_016137;
CC -!- DOMAIN: Contains a RS region (arginine-serine dipeptide repeat) within
CC the C-terminal domain which is the hallmark of the SR family of
CC splicing factors. This region probably plays a role in protein-protein
CC interactions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily.
CC {ECO:0000305}.
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DR EMBL; AABR03040241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC088316; AAH88316.1; -; mRNA.
DR RefSeq; NP_001013112.1; NM_001013094.1. [Q5I0H5-2]
DR RefSeq; XP_006239607.1; XM_006239545.3. [Q5I0H5-1]
DR AlphaFoldDB; Q5I0H5; -.
DR SMR; Q5I0H5; -.
DR STRING; 10116.ENSRNOP00000025531; -.
DR iPTMnet; Q5I0H5; -.
DR PhosphoSitePlus; Q5I0H5; -.
DR PaxDb; Q5I0H5; -.
DR PRIDE; Q5I0H5; -.
DR GeneID; 298686; -.
DR KEGG; rno:298686; -.
DR CTD; 81669; -.
DR RGD; 1309149; Ccnl2.
DR VEuPathDB; HostDB:ENSRNOG00000018691; -.
DR eggNOG; KOG0835; Eukaryota.
DR HOGENOM; CLU_022000_6_1_1; -.
DR InParanoid; Q5I0H5; -.
DR OrthoDB; 1519153at2759; -.
DR PhylomeDB; Q5I0H5; -.
DR TreeFam; TF101011; -.
DR PRO; PR:Q5I0H5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000018691; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; Q5I0H5; baseline and differential.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cyclin; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..520
FT /note="Cyclin-L2"
FT /id="PRO_0000080489"
FT REGION 81..183
FT /note="Cyclin-like 1"
FT REGION 196..280
FT /note="Cyclin-like 2"
FT REGION 309..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..422
FT /note="RS"
FT COMPBIAS 374..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S94"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S94"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S94"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S94"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 219..224
FT /note="NYMNDS -> VASEGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016136"
FT VAR_SEQ 225..520
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016137"
SQ SEQUENCE 520 AA; 58246 MW; CF78FB24BE3EFA7C CRC64;
MAAAAAGASG LMAPALAACS SGSGGAAPGS QGVLIGDRLY SGVLITLENC LLPDDKLRFT
PSMSSGLDID TETGLRVVGC ELIQAAGILL RLPQVAMATG QVLFQRFFYT KSFVKHSMEH
VSMACVHLAS KIEEAPRRIR DVINVFHRLR HLREKKKPVP LVLDQEYVNL KNQIIKAERR
VLKELGFCVH VKHPHKIIVM YLQVLECERN QHLVQTAWNY MNDSLRTDVF VRFQPESIAC
ACIYLAARTL EIPLPNRPHW FLLFGATEEE IQEICFKILQ LYTRKKVDLT HLESEVEKRK
HAIEEAKARA KGLLPPGSAP GLDSATAGFS PAPKPESPKE GKGSKSSPLS VKNAKRKMEG
PKKAKGDSPV NGLLKGQESR SQSRSREQSY SRSPSRSASP KRRKSDSGST SGGSKSQSRS
RSRSDSPPRQ VHRGAPYKGS EVRGSRKSKD CKHLTQKPHK SRSRSSSRSR SRSRERTDSS
GKYKKKSHYY RDQRRERSRS YERTGHRYER DHPGHSRHRR
