CCNL2_HUMAN
ID CCNL2_HUMAN Reviewed; 520 AA.
AC Q96S94; A0A024R072; A0A024R077; A0A0C4DGC4; A8K8A3; B1B152; F2Z3J5; Q5T2N5;
AC Q5T2N6; Q6IQ12; Q7Z4Z8; Q8N3C9; Q8N3D5; Q8NHE3; Q8TEL0; Q96B00;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cyclin-L2;
DE AltName: Full=Paneth cell-enhanced expression protein;
GN Name=CCNL2; ORFNames=SB138;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH POLR2A; CDC2L; SFRS2
RP AND SFRS7.
RC TISSUE=Bone marrow;
RX PubMed=14684736; DOI=10.1074/jbc.m312895200;
RA Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.;
RT "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in
RT pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma
RT cells.";
RL J. Biol. Chem. 279:11639-11648(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 3).
RC TISSUE=Bone, and Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-226 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 367-520 (ISOFORM 1/3).
RC TISSUE=Amygdala, and Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 324-520.
RA Zhao E.P., Yu L., Wan Y.Z., Tu Q., Zheng L.H., Zhao S.Y.;
RT "Cloning of a novel human cDNA homology to murine Paneth cell enhanced
RT expression mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, IDENTIFICATION OF ISOFORMS 1; 4 AND 5, INTERACTION WITH CDK11B
RP AND CKII, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18216018; DOI=10.1074/jbc.m708188200;
RA Loyer P., Trembley J.H., Grenet J.A., Busson A., Corlu A., Zhao W.,
RA Kocak M., Kidd V.J., Lahti J.M.;
RT "Characterization of cyclin L1 and L2 interactions with CDK11 and splicing
RT factors: influence of cyclin L isoforms on splice site selection.";
RL J. Biol. Chem. 283:7721-7732(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-348; SER-351 AND
RP SER-369, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-338 AND SER-369, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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:0000269|PubMed:14684736,
CC ECO:0000269|PubMed:18216018}.
CC -!- SUBUNIT: Interacts with CDK11A, CDK11B, CDK12, CDK13 and POLR2A, the
CC hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II
CC (PubMed:14684736, PubMed:18216018). May form a ternary complex with
CC CDK11B and casein kinase II (CKII) (PubMed:18216018). Interacts with
CC pre-mRNA-splicing factors, including at least SRSF1, SRSF2 AND
CC SRSF7/SLU7 (PubMed:14684736, PubMed:18216018).
CC {ECO:0000269|PubMed:14684736, ECO:0000269|PubMed:18216018}.
CC -!- INTERACTION:
CC Q96S94; Q59EK9: RUNDC3A; NbExp=3; IntAct=EBI-1045974, EBI-747225;
CC Q96S94-5; P50402: EMD; NbExp=3; IntAct=EBI-12024864, EBI-489887;
CC Q96S94-5; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-12024864, EBI-6658203;
CC Q96S94-5; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-12024864, EBI-10176379;
CC Q96S94-5; O15479: MAGEB2; NbExp=3; IntAct=EBI-12024864, EBI-1057615;
CC Q96S94-5; Q99750: MDFI; NbExp=3; IntAct=EBI-12024864, EBI-724076;
CC Q96S94-5; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-12024864, EBI-10232538;
CC Q96S94-5; Q59EK9-3: RUNDC3A; NbExp=3; IntAct=EBI-12024864, EBI-11957366;
CC Q96S94-5; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-12024864, EBI-725997;
CC Q96S94-5; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-12024864, EBI-14096082;
CC Q96S94-5; O15156-2: ZBTB7B; NbExp=3; IntAct=EBI-12024864, EBI-11522250;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:14684736,
CC ECO:0000269|PubMed:18216018}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:18216018}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=cyclin L2alpha;
CC IsoId=Q96S94-1; Sequence=Displayed;
CC Name=2; Synonyms=CCNL2s;
CC IsoId=Q96S94-2; Sequence=VSP_058302, VSP_058303;
CC Name=3;
CC IsoId=Q96S94-3; Sequence=VSP_016132;
CC Name=4; Synonyms=cyclin L2betaB;
CC IsoId=Q96S94-4; Sequence=VSP_058301, VSP_058304;
CC Name=5; Synonyms=cyclin L2betaA;
CC IsoId=Q96S94-5; Sequence=VSP_016130, VSP_016131;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14684736,
CC ECO:0000269|PubMed:18216018}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH71622.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB84938.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY037150; AAK67631.1; -; mRNA.
DR EMBL; AY116620; AAM76789.1; -; mRNA.
DR EMBL; AK074112; BAB84938.1; ALT_INIT; mRNA.
DR EMBL; AK056120; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK027770; BAG51376.1; -; mRNA.
DR EMBL; AK292268; BAF84957.1; -; mRNA.
DR EMBL; AL391244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR628411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56213.1; -; Genomic_DNA.
DR EMBL; CH471183; EAW56215.1; -; Genomic_DNA.
DR EMBL; CH471183; EAW56216.1; -; Genomic_DNA.
DR EMBL; CH471183; EAW56217.1; -; Genomic_DNA.
DR EMBL; BC016333; AAH16333.1; -; mRNA.
DR EMBL; BC071622; AAH71622.2; ALT_INIT; mRNA.
DR EMBL; AL834432; CAD39092.1; -; mRNA.
DR EMBL; AL834441; CAD39101.1; -; mRNA.
DR EMBL; AF087903; AAP97201.1; -; mRNA.
DR CCDS; CCDS30557.1; -. [Q96S94-1]
DR CCDS; CCDS30558.1; -. [Q96S94-5]
DR RefSeq; NP_001034666.1; NM_001039577.3. [Q96S94-5]
DR RefSeq; NP_001307082.1; NM_001320153.1. [Q96S94-3]
DR RefSeq; NP_001307084.1; NM_001320155.1. [Q96S94-3]
DR RefSeq; NP_112199.2; NM_030937.4. [Q96S94-1]
DR RefSeq; XP_011540523.1; XM_011542221.2.
DR RefSeq; XP_016857911.1; XM_017002422.1.
DR AlphaFoldDB; Q96S94; -.
DR SMR; Q96S94; -.
DR BioGRID; 123566; 90.
DR ComplexPortal; CPX-343; Cyclin L2-CDK11A(p110) complex.
DR ComplexPortal; CPX-345; Cyclin L2-CDK11B(p58) complex.
DR ComplexPortal; CPX-347; Cyclin L2-CDK11A(p58) complex.
DR ComplexPortal; CPX-349; Cyclin L2-CDK11B(p110) complex.
DR IntAct; Q96S94; 51.
DR MINT; Q96S94; -.
DR STRING; 9606.ENSP00000383611; -.
DR GlyGen; Q96S94; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96S94; -.
DR PhosphoSitePlus; Q96S94; -.
DR BioMuta; CCNL2; -.
DR DMDM; 74752124; -.
DR EPD; Q96S94; -.
DR jPOST; Q96S94; -.
DR MassIVE; Q96S94; -.
DR MaxQB; Q96S94; -.
DR PaxDb; Q96S94; -.
DR PeptideAtlas; Q96S94; -.
DR PRIDE; Q96S94; -.
DR ProteomicsDB; 23998; -.
DR ProteomicsDB; 78087; -. [Q96S94-1]
DR ProteomicsDB; 78088; -. [Q96S94-2]
DR ProteomicsDB; 78089; -. [Q96S94-3]
DR TopDownProteomics; Q96S94-1; -. [Q96S94-1]
DR Antibodypedia; 26320; 132 antibodies from 26 providers.
DR DNASU; 81669; -.
DR Ensembl; ENST00000400809.8; ENSP00000383611.3; ENSG00000221978.13. [Q96S94-1]
DR Ensembl; ENST00000408918.8; ENSP00000386158.4; ENSG00000221978.13. [Q96S94-5]
DR Ensembl; ENST00000481223.6; ENSP00000423734.1; ENSG00000221978.13. [Q96S94-4]
DR Ensembl; ENST00000488340.5; ENSP00000424647.1; ENSG00000221978.13. [Q96S94-2]
DR GeneID; 81669; -.
DR KEGG; hsa:81669; -.
DR MANE-Select; ENST00000400809.8; ENSP00000383611.3; NM_030937.6; NP_112199.2.
DR UCSC; uc001afi.3; human. [Q96S94-1]
DR UCSC; uc057beg.1; human.
DR CTD; 81669; -.
DR DisGeNET; 81669; -.
DR GeneCards; CCNL2; -.
DR HGNC; HGNC:20570; CCNL2.
DR HPA; ENSG00000221978; Low tissue specificity.
DR MIM; 613482; gene.
DR neXtProt; NX_Q96S94; -.
DR OpenTargets; ENSG00000221978; -.
DR PharmGKB; PA134973681; -.
DR VEuPathDB; HostDB:ENSG00000221978; -.
DR eggNOG; KOG0835; Eukaryota.
DR GeneTree; ENSGT00940000159239; -.
DR HOGENOM; CLU_022000_6_1_1; -.
DR InParanoid; Q96S94; -.
DR OMA; KYPAQKP; -.
DR OrthoDB; 1519153at2759; -.
DR PhylomeDB; Q96S94; -.
DR TreeFam; TF101011; -.
DR PathwayCommons; Q96S94; -.
DR SignaLink; Q96S94; -.
DR SIGNOR; Q96S94; -.
DR BioGRID-ORCS; 81669; 39 hits in 1090 CRISPR screens.
DR ChiTaRS; CCNL2; human.
DR GeneWiki; CCNL2; -.
DR GenomeRNAi; 81669; -.
DR Pharos; Q96S94; Tbio.
DR PRO; PR:Q96S94; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96S94; protein.
DR Bgee; ENSG00000221978; Expressed in right uterine tube and 181 other tissues.
DR ExpressionAtlas; Q96S94; baseline and differential.
DR Genevisible; Q96S94; HS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IC:ComplexPortal.
DR GO; GO:0046605; P:regulation of centrosome cycle; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:ComplexPortal.
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 Acetylation; Alternative splicing; Cyclin; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..520
FT /note="Cyclin-L2"
FT /id="PRO_0000080487"
FT REGION 83..185
FT /note="Cyclin-like 1"
FT REGION 198..282
FT /note="Cyclin-like 2"
FT REGION 316..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..423
FT /note="RS"
FT COMPBIAS 405..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..458
FT /note="Basic and acidic 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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..222
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016132"
FT VAR_SEQ 221..236
FT /note="NYMNDSLRTDVFVRFQ -> VASEDPLLKWDSWQRL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_058301"
FT VAR_SEQ 221..227
FT /note="NYMNDSL -> VASEGIT (in isoform 2)"
FT /id="VSP_058302"
FT VAR_SEQ 221..226
FT /note="NYMNDS -> VASEGK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14684736,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.2"
FT /id="VSP_016130"
FT VAR_SEQ 227..520
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14684736,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.2"
FT /id="VSP_016131"
FT VAR_SEQ 228..520
FT /note="Missing (in isoform 2)"
FT /id="VSP_058303"
FT VAR_SEQ 237..520
FT /note="Missing (in isoform 4)"
FT /id="VSP_058304"
FT CONFLICT 71
FT /note="T -> S (in Ref. 6; AAH16333)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..325
FT /note="DG -> MS (in Ref. 8; AAP97201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 58147 MW; 4341E55D03D7B0E0 CRC64;
MAAAAAAAGA AGSAAPAAAA GAPGSGGAPS GSQGVLIGDR LYSGVLITLE NCLLPDDKLR
FTPSMSSGLD TDTETDLRVV GCELIQAAGI LLRLPQVAMA TGQVLFQRFF YTKSFVKHSM
EHVSMACVHL ASKIEEAPRR IRDVINVFHR LRQLRDKKKP VPLLLDQDYV NLKNQIIKAE
RRVLKELGFC VHVKHPHKII VMYLQVLECE RNQHLVQTSW NYMNDSLRTD VFVRFQPESI
ACACIYLAAR TLEIPLPNRP HWFLLFGATE EEIQEICLKI LQLYARKKVD LTHLEGEVEK
RKHAIEEAKA QARGLLPGGT QVLDGTSGFS PAPKLVESPK EGKGSKPSPL SVKNTKRRLE
GAKKAKADSP VNGLPKGRES RSRSRSREQS YSRSPSRSAS PKRRKSDSGS TSGGSKSQSR
SRSRSDSPPR QAPRSAPYKG SEIRGSRKSK DCKYPQKPHK SRSRSSSRSR SRSRERADNP
GKYKKKSHYY RDQRRERSRS YERTGRRYER DHPGHSRHRR
