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 27-MAR-2024, entry version 189. 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). RN [21] RP INTERACTION WITH HHV-1 TRANSCRIPTIONAL REGULATOR ICP22 (MICROBIAL RP INFECTION). RX PubMed=34696162; DOI=10.3390/vaccines9101054; RA Isa N.F., Bensaude O., Aziz N.C., Murphy S.; RT "HSV-1 ICP22 Is a Selective Viral Repressor of Cellular RNA Polymerase II- RT Mediated Transcription Elongation."; RL Vaccines (Basel) 9:0-0(2021). 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: (Microbial infection) Interacts with human herpes virus 1 CC (HHV-1) transcriptional regulator ICP22. {ECO:0000269|PubMed:34696162}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 56. 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; 46. 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; 9606-ENSP00000295926; -. DR PeptideAtlas; Q9UK58; -. DR ProteomicsDB; 11129; -. DR ProteomicsDB; 84724; -. [Q9UK58-1] DR ProteomicsDB; 84725; -. [Q9UK58-4] DR ProteomicsDB; 84726; -. [Q9UK58-5] DR Pumba; Q9UK58; -. DR Antibodypedia; 18411; 255 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 AGR; HGNC:20569; -. 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; GHKHRDG; -. DR OrthoDB; 4848076at2759; -. DR PhylomeDB; Q9UK58; -. DR TreeFam; TF101011; -. DR PathwayCommons; Q9UK58; -. DR SignaLink; Q9UK58; -. DR BioGRID-ORCS; 57018; 343 hits in 1164 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 197 other cell types or tissues. DR ExpressionAtlas; Q9UK58; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0051726; P:regulation of cell cycle; NAS:ComplexPortal. DR GO; GO:0046605; P:regulation of centrosome cycle; NAS: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 Gene3D; 1.10.472.10; Cyclin-like; 2. DR InterPro; IPR013763; Cyclin-like_dom. 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; CYCLIN; 1. DR PANTHER; PTHR10026:SF64; CYCLIN-L1; 1. DR Pfam; PF02984; Cyclin_C; 1. DR Pfam; PF00134; Cyclin_N; 1. DR PIRSF; PIRSF036580; Cyclin_L; 1. DR SMART; SM00385; CYCLIN; 2. DR SMART; SM01332; Cyclin_C; 1. DR SUPFAM; SSF47954; Cyclin-like; 2. DR Genevisible; Q9UK58; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cyclin; Host-virus interaction; Isopeptide bond; KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; KW Transcription; 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 //