CCNL1_HUMAN
ID CCNL1_HUMAN Reviewed; 526 AA.
AC Q9UK58; B3KMY3; C9JPL0; Q6NVY9; Q6UWS7; Q8NI48; Q96QT0; Q9NZF3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Cyclin-L1;
DE Short=Cyclin-L;
GN Name=CCNL1; ORFNames=BM-001, UNQ530/PRO1073;
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; 2 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, DOMAIN, AND INTERACTION WITH CDC2L AND SFRS2.
RC TISSUE=Lung;
RX PubMed=11980906; DOI=10.1074/jbc.m202266200;
RA Dickinson L.A., Edgar A.J., Ehley J., Gottesfeld J.M.;
RT "Cyclin L is an RS domain protein involved in pre-mRNA splicing.";
RL J. Biol. Chem. 277:25465-25473(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Lung, and Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-526 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 226-526 (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12414649;
RA Redon R., Hussenet T., Bour G., Caulee K., Jost B., Muller D.,
RA Abecassis J., du Manoir S.;
RT "Amplicon mapping and transcriptional analysis pinpoint cyclin L as a
RT candidate oncogene in head and neck cancer.";
RL Cancer Res. 62:6211-6217(2002).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15700036; DOI=10.1038/sj.bjc.6602400;
RA Sticht C., Hofele C., Flechtenmacher C., Bosch F.X., Freier K., Lichter P.,
RA Joos S.;
RT "Amplification of Cyclin L1 is associated with lymph node metastases in
RT head and neck squamous cell carcinoma (HNSCC).";
RL Br. J. Cancer 92:770-774(2005).
RN [10]
RP FUNCTION, IDENTIFICATION OF ISOFORMS 1; 2 AND 3, INTERACTION WITH CDK11B;
RP CKII; SRSF1 AND SRSF7/SLU7, 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-325; SER-335 AND SER-338, AND
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-338 AND SER-352, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-352 AND SER-445, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352; SER-355 AND SER-374, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP 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).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-362, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-339 AND LYS-347, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing. Functions in association with
CC cyclin-dependent kinases (CDKs) (PubMed:18216018). Inhibited by the
CC CDK-specific inhibitor CDKN1A/p21 (PubMed:11980906). May play a role in
CC the regulation of RNA polymerase II (pol II). May be a candidate proto-
CC oncogene in head and neck squamous cell carcinomas (HNSCC)
CC (PubMed:12414649, PubMed:15700036). {ECO:0000269|PubMed:11980906,
CC ECO:0000269|PubMed:12414649, ECO:0000269|PubMed:15700036,
CC ECO:0000269|PubMed:18216018}.
CC -!- SUBUNIT: Interacts with POLR2A via its hyperphosphorylated C-terminal
CC domain (CTD) (By similarity). Interacts with CDK11A, CDK12 and CDK13
CC (PubMed:11980906, PubMed:18216018). Isoforms 1 and 2, but not isoform
CC 3, interact with CDK11B. May form a ternary complex with CDK11B and
CC casein kinase II (CKII) (PubMed:18216018). Interacts with pre-mRNA-
CC splicing factors, including at least SRSF1, SRSF2 AND SRSF7/SLU7
CC (PubMed:11980906, PubMed:18216018). {ECO:0000250|UniProtKB:Q9R1Q2,
CC ECO:0000269|PubMed:11980906, ECO:0000269|PubMed:18216018}.
CC -!- INTERACTION:
CC Q9UK58; Q92624: APPBP2; NbExp=3; IntAct=EBI-2836773, EBI-743771;
CC Q9UK58; Q6NVI2: CASP8; NbExp=3; IntAct=EBI-2836773, EBI-12861768;
CC Q9UK58; Q92997: DVL3; NbExp=3; IntAct=EBI-2836773, EBI-739789;
CC Q9UK58; Q8N9E0: FAM133A; NbExp=3; IntAct=EBI-2836773, EBI-10268158;
CC Q9UK58; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-2836773, EBI-10176379;
CC Q9UK58; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-2836773, EBI-742459;
CC Q9UK58; Q6ZUT1: NKAPD1; NbExp=6; IntAct=EBI-2836773, EBI-3920396;
CC Q9UK58; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-2836773, EBI-11320284;
CC Q9UK58; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-2836773, EBI-5280197;
CC Q9UK58; O75771: RAD51D; NbExp=3; IntAct=EBI-2836773, EBI-1055693;
CC Q9UK58; Q15287: RNPS1; NbExp=4; IntAct=EBI-2836773, EBI-395959;
CC Q9UK58; Q9BUV0: RSRP1; NbExp=3; IntAct=EBI-2836773, EBI-745604;
CC Q9UK58; Q9UHR5: SAP30BP; NbExp=3; IntAct=EBI-2836773, EBI-751683;
CC Q9UK58; O60504: SORBS3; NbExp=3; IntAct=EBI-2836773, EBI-741237;
CC Q9UK58; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-2836773, EBI-10268630;
CC Q9UK58; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2836773, EBI-1105213;
CC Q9UK58; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-2836773, EBI-527853;
CC Q9UK58; Q15696: ZRSR2; NbExp=3; IntAct=EBI-2836773, EBI-6657923;
CC Q9UK58-5; O94985-2: CLSTN1; NbExp=3; IntAct=EBI-25873837, EBI-16041593;
CC Q9UK58-5; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25873837, EBI-21591415;
CC Q9UK58-5; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-25873837, EBI-5280197;
CC Q9UK58-5; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-25873837, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:18216018}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:18216018}. Note=Found in
CC nuclear intrachromatin granules clusters (IGC), also called nuclear
CC speckles, which are storage compartments for nuclear proteins involved
CC in mRNA processing. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Ccnl1 is an immediate-early gene with independently regulated
CC isoforms.;
CC Name=1; Synonyms=Cyclin L alpha, cyclin L1alpha;
CC IsoId=Q9UK58-1; Sequence=Displayed;
CC Name=2; Synonyms=Cyclin L beta, cyclin L1beta;
CC IsoId=Q9UK58-4; Sequence=VSP_016122, VSP_016123;
CC Name=3; Synonyms=Cyclin L gamma, cyclin L1gamma;
CC IsoId=Q9UK58-5; Sequence=VSP_016120, VSP_016121;
CC Name=4;
CC IsoId=Q9UK58-6; Sequence=VSP_058299, VSP_058300;
CC -!- TISSUE SPECIFICITY: Widely expressed. Overexpression in primary tumors
CC of head and neck squamous cell carcinomas (HNSCC).
CC {ECO:0000269|PubMed:11980906, ECO:0000269|PubMed:12414649,
CC ECO:0000269|PubMed:15700036, 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. {ECO:0000269|PubMed:11980906}.
CC -!- MISCELLANEOUS: CCNL1 is amplified in several HNSCC. May play a critical
CC role in the formation of loco-regional metastases and an unfavorable
CC clinical outcome of HNSCC.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin L subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF64257.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAQ89026.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF180920; AAD53184.1; -; mRNA.
DR EMBL; AF367476; AAM21204.1; -; mRNA.
DR EMBL; AF367477; AAM21205.1; -; mRNA.
DR EMBL; AY034790; AAK61551.1; -; mRNA.
DR EMBL; AK022974; BAG51145.1; -; mRNA.
DR EMBL; AK122738; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC104411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78712.1; -; Genomic_DNA.
DR EMBL; BC007081; AAH07081.1; -; mRNA.
DR EMBL; BC038394; AAH38394.1; -; mRNA.
DR EMBL; BC067812; AAH67812.1; -; mRNA.
DR EMBL; AF208843; AAF64257.1; ALT_SEQ; mRNA.
DR EMBL; AY358663; AAQ89026.1; ALT_SEQ; mRNA.
DR CCDS; CCDS3178.1; -. [Q9UK58-1]
DR CCDS; CCDS77847.1; -. [Q9UK58-6]
DR RefSeq; NP_001295114.1; NM_001308185.1. [Q9UK58-6]
DR RefSeq; NP_064703.1; NM_020307.3. [Q9UK58-1]
DR RefSeq; XP_016862381.1; XM_017006892.1.
DR RefSeq; XP_016862382.1; XM_017006893.1.
DR RefSeq; XP_016862383.1; XM_017006894.1.
DR RefSeq; XP_016862384.1; XM_017006895.1.
DR RefSeq; XP_016862385.1; XM_017006896.1.
DR AlphaFoldDB; Q9UK58; -.
DR SMR; Q9UK58; -.
DR BioGRID; 121327; 46.
DR ComplexPortal; CPX-341; Cyclin L1-CDK11A(p110) complex.
DR ComplexPortal; CPX-344; Cyclin L1-CDK11A(p58) complex.
DR ComplexPortal; CPX-346; Cyclin L1-CDK11B(p58) complex.
DR ComplexPortal; CPX-348; Cyclin L1-CDK11B(p110) complex.
DR IntAct; Q9UK58; 45.
DR MINT; Q9UK58; -.
DR STRING; 9606.ENSP00000295926; -.
DR GlyGen; Q9UK58; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UK58; -.
DR PhosphoSitePlus; Q9UK58; -.
DR BioMuta; CCNL1; -.
DR DMDM; 74753368; -.
DR EPD; Q9UK58; -.
DR jPOST; Q9UK58; -.
DR MassIVE; Q9UK58; -.
DR MaxQB; Q9UK58; -.
DR PaxDb; Q9UK58; -.
DR PeptideAtlas; Q9UK58; -.
DR PRIDE; Q9UK58; -.
DR ProteomicsDB; 11129; -.
DR ProteomicsDB; 84724; -. [Q9UK58-1]
DR ProteomicsDB; 84725; -. [Q9UK58-4]
DR ProteomicsDB; 84726; -. [Q9UK58-5]
DR Antibodypedia; 18411; 233 antibodies from 34 providers.
DR DNASU; 57018; -.
DR Ensembl; ENST00000295925.5; ENSP00000295925.4; ENSG00000163660.12. [Q9UK58-5]
DR Ensembl; ENST00000295926.8; ENSP00000295926.4; ENSG00000163660.12. [Q9UK58-1]
DR Ensembl; ENST00000461804.5; ENSP00000420277.1; ENSG00000163660.12. [Q9UK58-6]
DR Ensembl; ENST00000465947.5; ENSP00000418094.1; ENSG00000163660.12. [Q9UK58-5]
DR Ensembl; ENST00000470121.5; ENSP00000417237.1; ENSG00000163660.12. [Q9UK58-4]
DR Ensembl; ENST00000475298.5; ENSP00000417343.1; ENSG00000163660.12. [Q9UK58-5]
DR Ensembl; ENST00000477127.5; ENSP00000418449.1; ENSG00000163660.12. [Q9UK58-5]
DR Ensembl; ENST00000631619.1; ENSP00000487951.1; ENSG00000163660.12. [Q9UK58-5]
DR GeneID; 57018; -.
DR KEGG; hsa:57018; -.
DR MANE-Select; ENST00000295926.8; ENSP00000295926.4; NM_020307.4; NP_064703.1.
DR UCSC; uc003fbd.2; human.
DR UCSC; uc003fbf.4; human. [Q9UK58-1]
DR CTD; 57018; -.
DR DisGeNET; 57018; -.
DR GeneCards; CCNL1; -.
DR HGNC; HGNC:20569; CCNL1.
DR HPA; ENSG00000163660; Low tissue specificity.
DR MIM; 613384; gene.
DR neXtProt; NX_Q9UK58; -.
DR OpenTargets; ENSG00000163660; -.
DR VEuPathDB; HostDB:ENSG00000163660; -.
DR eggNOG; KOG0835; Eukaryota.
DR GeneTree; ENSGT00940000159135; -.
DR HOGENOM; CLU_107641_0_0_1; -.
DR InParanoid; Q9UK58; -.
DR OMA; RCHMVQE; -.
DR OrthoDB; 1519153at2759; -.
DR PhylomeDB; Q9UK58; -.
DR TreeFam; TF101011; -.
DR PathwayCommons; Q9UK58; -.
DR SignaLink; Q9UK58; -.
DR BioGRID-ORCS; 57018; 338 hits in 1086 CRISPR screens.
DR ChiTaRS; CCNL1; human.
DR GeneWiki; CCNL1; -.
DR GenomeRNAi; 57018; -.
DR Pharos; Q9UK58; Tbio.
DR PRO; PR:Q9UK58; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UK58; protein.
DR Bgee; ENSG00000163660; Expressed in mucosa of stomach and 195 other tissues.
DR ExpressionAtlas; Q9UK58; baseline and differential.
DR Genevisible; Q9UK58; HS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:InterPro.
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 GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; IPR015431; Cyclin_L1.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR PANTHER; PTHR10026:SF64; PTHR10026:SF64; 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; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..526
FT /note="Cyclin-L1"
FT /id="PRO_0000080480"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..190
FT /note="Cyclin-like 1"
FT REGION 203..287
FT /note="Cyclin-like 2"
FT REGION 318..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..432
FT /note="RS"
FT COMPBIAS 343..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..416
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..526
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 352
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 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 347
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297"
FT VAR_SEQ 163..172
FT /note="RTPSPLILDQ -> SDQLHLPKPG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11980906"
FT /id="VSP_016120"
FT VAR_SEQ 173..526
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11980906"
FT /id="VSP_016121"
FT VAR_SEQ 226..232
FT /note="NYMNDSL -> VVHDGKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11980906"
FT /id="VSP_016122"
FT VAR_SEQ 233..526
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11980906"
FT /id="VSP_016123"
FT VAR_SEQ 411..428
FT /note="HYNNRRSRSGTYSSRSRS -> QDEVLLRCPGRSRTPGLK (in isoform
FT 4)"
FT /id="VSP_058299"
FT VAR_SEQ 429..526
FT /note="Missing (in isoform 4)"
FT /id="VSP_058300"
FT CONFLICT 149
FT /note="V -> L (in Ref. 5; AAH67812)"
FT /evidence="ECO:0000305"
FT CONFLICT 507..508
FT /note="RS -> SP (in Ref. 6; AAF64257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59634 MW; 64C0CAEF54A3E9F9 CRC64;
MASGPHSTAT AAAAASSAAP SAGGSSSGTT TTTTTTTGGI LIGDRLYSEV SLTIDHSLIP
EERLSPTPSM QDGLDLPSET DLRILGCELI QAAGILLRLP QVAMATGQVL FHRFFYSKSF
VKHSFEIVAM ACINLASKIE EAPRRIRDVI NVFHHLRQLR GKRTPSPLIL DQNYINTKNQ
VIKAERRVLK ELGFCVHVKH PHKIIVMYLQ VLECERNQTL VQTAWNYMND SLRTNVFVRF
QPETIACACI YLAARALQIP LPTRPHWFLL FGTTEEEIQE ICIETLRLYT RKKPNYELLE
KEVEKRKVAL QEAKLKAKGL NPDGTPALST LGGFSPASKP SSPREVKAEE KSPISINVKT
VKKEPEDRQQ ASKSPYNGVR KDSKRSRNSR SASRSRSRTR SRSRSHTPRR HYNNRRSRSG
TYSSRSRSRS RSHSESPRRH HNHGSPHLKA KHTRDDLKSS NRHGHKRKKS RSRSQSKSRD
HSDAAKKHRH ERGHHRDRRE RSRSFERSHK SKHHGGSRSG HGRHRR
