CCNT2_HUMAN
ID CCNT2_HUMAN Reviewed; 730 AA.
AC O60583; A8KA48; D3DP73; D3DP74; O60582; Q29R66; Q53SR4; Q5I1Y0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Cyclin-T2 {ECO:0000250|UniProtKB:Q7TQK0};
DE Short=CycT2 {ECO:0000250|UniProtKB:Q7TQK0};
GN Name=CCNT2 {ECO:0000312|HGNC:HGNC:1600};
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), INTERACTION WITH CDK9,
RP IDENTIFICATION OF P-TEFB COMPLEX, TISSUE SPECIFICITY, AND FUNCTION OF
RP P-TEFB COMPLEX.
RC TISSUE=Brain;
RX PubMed=9499409; DOI=10.1101/gad.12.5.755;
RA Peng J.-M., Zhu Y., Milton J.T., Price D.H.;
RT "Identification of multiple cyclin subunits of human P-TEFb.";
RL Genes Dev. 12:755-762(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP INTERACTION WITH HIV-2 AND SIV TAT (MICROBIAL INFECTION), AND MUTAGENESIS
RP OF ASN-260.
RX PubMed=10364329; DOI=10.1128/jvi.73.7.5777-5786.1999;
RA Bieniasz P.D., Grdina T.A., Bogerd H.P., Cullen B.R.;
RT "Analysis of the effect of natural sequence variation in Tat and in cyclin
RT T on the formation and RNA binding properties of Tat-cyclin T complexes.";
RL J. Virol. 73:5777-5786(1999).
RN [8]
RP FUNCTION.
RX PubMed=11713533; DOI=10.1038/35104581;
RA Nguyen V.T., Kiss T., Michels A.A., Bensaude O.;
RT "7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T
RT complexes.";
RL Nature 414:322-325(2001).
RN [9]
RP INTERACTION WITH RB1.
RX PubMed=12037672; DOI=10.1038/sj.onc.1205511;
RA Simone C., Bagella L., Bellan C., Giordano A.;
RT "Physical interaction between pRb and cdk9/cyclinT2 complex.";
RL Oncogene 21:4158-4165(2002).
RN [10]
RP INTERACTION WITH POLR2A, FUNCTION, AND REGION.
RX PubMed=15563843; DOI=10.1016/j.gene.2004.08.027;
RA Kurosu T., Zhang F., Peterlin B.M.;
RT "Transcriptional activity and substrate recognition of cyclin T2 from P-
RT TEFb.";
RL Gene 343:173-179(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH CDK9 AND PKN1.
RX PubMed=16331689; DOI=10.1002/jcp.20566;
RA Cottone G., Baldi A., Palescandolo E., Manente L., Penta R., Paggi M.G.,
RA De Luca A.;
RT "Pkn is a novel partner of cyclin T2a in muscle differentiation.";
RL J. Cell. Physiol. 207:232-237(2006).
RN [12]
RP INTERACTION WITH MDFI AND MDFIC, AND REGION.
RX PubMed=17289077; DOI=10.1016/j.jmb.2007.01.020;
RA Wang Q., Young T.M., Mathews M.B., Pe'ery T.;
RT "Developmental regulators containing the I-mfa domain interact with T
RT cyclins and Tat and modulate transcription.";
RL J. Mol. Biol. 367:630-646(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, 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 [18]
RP INTERACTION WITH HEXIM1 AND HEXIM2.
RX PubMed=19883659; DOI=10.1016/j.jmb.2009.10.055;
RA Czudnochowski N., Vollmuth F., Baumann S., Vogel-Bachmayr K., Geyer M.;
RT "Specificity of Hexim1 and Hexim2 complex formation with cyclin T1/T2,
RT importin alpha and 7SK snRNA.";
RL J. Mol. Biol. 395:28-41(2010).
RN [19]
RP INTERACTION WITH MON1B, AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=21509660; DOI=10.1007/s11427-011-4160-3;
RA Wu W., Yu X., Li W., Guo L., Liu L., Wang L., Li Q.;
RT "HSV-1 stimulation-related protein HSRG1 inhibits viral gene
RT transcriptional elongation by interacting with Cyclin T2.";
RL Sci. China Life Sci. 54:359-365(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP 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 [22]
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).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-407, AND IDENTIFICATION BY MASS
RP 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: Regulatory subunit of the cyclin-dependent kinase pair
CC (CDK9/cyclin T) complex, also called positive transcription elongation
CC factor B (P-TEFB), which is proposed to facilitate the transition from
CC abortive to production elongation by phosphorylating the CTD (carboxy-
CC terminal domain) of the large subunit of RNA polymerase II (RNAP II)
CC (PubMed:9499409, PubMed:15563843). The activity of this complex is
CC regulated by binding with 7SK snRNA (PubMed:11713533). Plays a role
CC during muscle differentiation; P-TEFB complex interacts with MYOD1;
CC this tripartite complex promotes the transcriptional activity of MYOD1
CC through its CDK9-mediated phosphorylation and binds the chromatin of
CC promoters and enhancers of muscle-specific genes; this event correlates
CC with hyperphosphorylation of the CTD domain of RNA pol II (By
CC similarity). In addition, enhances MYOD1-dependent transcription
CC through interaction with PKN1 (PubMed:16331689). Involved in early
CC embryo development (By similarity). {ECO:0000250|UniProtKB:Q7TQK0,
CC ECO:0000269|PubMed:11713533, ECO:0000269|PubMed:15563843,
CC ECO:0000269|PubMed:16331689, ECO:0000269|PubMed:9499409}.
CC -!- FUNCTION: (Microbial infection) Promotes transcriptional activation of
CC early and late herpes simplex virus 1/HHV-1 promoters.
CC {ECO:0000269|PubMed:21509660}.
CC -!- SUBUNIT: Interacts with CDK9 to form P-TEFb (PubMed:9499409,
CC PubMed:16331689). Interacts with POLR2A (via the C-terminal domain
CC (CTD)); mediates transcriptional activity (PubMed:15563843). Interacts
CC with HEXIM1; mediates formation of a tripartite complex with KPNA2.
CC Interacts with HEXIM2 (PubMed:19883659). Interacts with PKN1; enhances
CC MYOD1-dependent transcription (PubMed:16331689). P-TEFB complex
CC interacts with RB1; promotes phosphorylation of RB1 (PubMed:12037672).
CC P-TEFB complex interacts with MYOD1; promotes the transcriptional
CC activity of MYOD1 through its CDK9-mediated phosphorylation (By
CC similarity). Interacts with MDFI and MDFIC (PubMed:17289077). Interacts
CC with MON1B; down-regulates CCNT2-mediated activation of viral promoters
CC during herpes simplex virus 1/HHV-1 infection (PubMed:21509660).
CC {ECO:0000250|UniProtKB:Q7TQK0, ECO:0000269|PubMed:12037672,
CC ECO:0000269|PubMed:15563843, ECO:0000269|PubMed:16331689,
CC ECO:0000269|PubMed:17289077, ECO:0000269|PubMed:19883659,
CC ECO:0000269|PubMed:21509660, ECO:0000269|PubMed:9499409}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-2 and SIV Tat. Does
CC not bind efficiently to the transactivation domain of the HIV-1 Tat
CC (PubMed:10364329). {ECO:0000269|PubMed:10364329}.
CC -!- INTERACTION:
CC O60583; P50750: CDK9; NbExp=6; IntAct=EBI-2836757, EBI-1383449;
CC O60583-1; P50750: CDK9; NbExp=2; IntAct=EBI-9077118, EBI-1383449;
CC O60583-2; P50750: CDK9; NbExp=3; IntAct=EBI-9077112, EBI-1383449;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q7TQK0}. Nucleus {ECO:0000250|UniProtKB:Q7TQK0}.
CC Note=Nucleus in differentiating cells. {ECO:0000250|UniProtKB:Q7TQK0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=B;
CC IsoId=O60583-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=O60583-2; Sequence=VSP_001258;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9499409}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ccnt2/";
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DR EMBL; AF048731; AAC39665.1; -; mRNA.
DR EMBL; AF048732; AAC39666.1; -; mRNA.
DR EMBL; AY865621; AAW56073.1; -; Genomic_DNA.
DR EMBL; AK292913; BAF85602.1; -; mRNA.
DR EMBL; AC016725; AAY14998.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11644.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11645.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11646.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11647.1; -; Genomic_DNA.
DR EMBL; BC114366; AAI14367.1; -; mRNA.
DR CCDS; CCDS2174.1; -. [O60583-1]
DR CCDS; CCDS2175.1; -. [O60583-2]
DR RefSeq; NP_001232.1; NM_001241.3. [O60583-2]
DR RefSeq; NP_490595.1; NM_058241.2. [O60583-1]
DR PDB; 2IVX; X-ray; 1.80 A; A/B=7-263.
DR PDBsum; 2IVX; -.
DR AlphaFoldDB; O60583; -.
DR SMR; O60583; -.
DR BioGRID; 107344; 51.
DR ComplexPortal; CPX-321; Positive transcription elongation factor B, CDK9-cyclinT2a complex. [O60583-2]
DR ComplexPortal; CPX-322; Positive transcription elongation factor B, CDK9-cyclinT2b complex. [O60583-1]
DR CORUM; O60583; -.
DR ELM; O60583; -.
DR IntAct; O60583; 22.
DR MINT; O60583; -.
DR STRING; 9606.ENSP00000264157; -.
DR BindingDB; O60583; -.
DR ChEMBL; CHEMBL1293321; -.
DR iPTMnet; O60583; -.
DR PhosphoSitePlus; O60583; -.
DR BioMuta; CCNT2; -.
DR EPD; O60583; -.
DR jPOST; O60583; -.
DR MassIVE; O60583; -.
DR MaxQB; O60583; -.
DR PaxDb; O60583; -.
DR PeptideAtlas; O60583; -.
DR PRIDE; O60583; -.
DR ProteomicsDB; 49477; -. [O60583-1]
DR ProteomicsDB; 49478; -. [O60583-2]
DR Antibodypedia; 1420; 111 antibodies from 27 providers.
DR DNASU; 905; -.
DR Ensembl; ENST00000264157.10; ENSP00000264157.5; ENSG00000082258.13. [O60583-1]
DR Ensembl; ENST00000295238.10; ENSP00000295238.6; ENSG00000082258.13. [O60583-2]
DR GeneID; 905; -.
DR KEGG; hsa:905; -.
DR MANE-Select; ENST00000264157.10; ENSP00000264157.5; NM_058241.3; NP_490595.1.
DR UCSC; uc002tub.3; human. [O60583-1]
DR CTD; 905; -.
DR DisGeNET; 905; -.
DR GeneCards; CCNT2; -.
DR HGNC; HGNC:1600; CCNT2.
DR HPA; ENSG00000082258; Low tissue specificity.
DR MIM; 603862; gene.
DR neXtProt; NX_O60583; -.
DR OpenTargets; ENSG00000082258; -.
DR PharmGKB; PA26164; -.
DR VEuPathDB; HostDB:ENSG00000082258; -.
DR eggNOG; KOG0834; Eukaryota.
DR GeneTree; ENSGT00940000155759; -.
DR HOGENOM; CLU_012994_1_1_1; -.
DR InParanoid; O60583; -.
DR OMA; DGNHEYS; -.
DR PhylomeDB; O60583; -.
DR TreeFam; TF101014; -.
DR PathwayCommons; O60583; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; O60583; -.
DR BioGRID-ORCS; 905; 30 hits in 1092 CRISPR screens.
DR ChiTaRS; CCNT2; human.
DR EvolutionaryTrace; O60583; -.
DR GeneWiki; Cyclin_T2; -.
DR GenomeRNAi; 905; -.
DR Pharos; O60583; Tbio.
DR PRO; PR:O60583; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O60583; protein.
DR Bgee; ENSG00000082258; Expressed in adrenal tissue and 198 other tissues.
DR ExpressionAtlas; O60583; baseline and differential.
DR Genevisible; O60583; HS.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0097322; F:7SK snRNA binding; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; IPI:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0019085; P:early viral transcription; IDA:UniProtKB.
DR GO; GO:0019086; P:late viral transcription; IDA:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0051147; P:regulation of muscle cell differentiation; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR028862; CCNT2.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR PANTHER; PTHR10026:SF43; PTHR10026:SF43; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cyclin;
KW Cytoplasm; Host-virus interaction; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..730
FT /note="Cyclin-T2"
FT /id="PRO_0000080495"
FT DOMAIN 12..147
FT /note="Cyclin N-terminal"
FT /evidence="ECO:0000255"
FT REGION 1..300
FT /note="Interaction with MDFIC and MDFI"
FT /evidence="ECO:0000269|PubMed:17289077"
FT REGION 250..300
FT /note="Interaction with POLR2A"
FT /evidence="ECO:0000269|PubMed:15563843"
FT REGION 341..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..576
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 643..730
FT /note="SSSSSSSSVKQYISSHNSVFNHPLPPPPPVTYQVGYGHLSTLVKLDKKPVET
FT NGPDANHEYSTSSQHMDYKDTFDMLDSLLSAQGMNM -> GLRTSQHPRETGQEASGDQ
FT RS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9499409"
FT /id="VSP_001258"
FT MUTAGEN 260
FT /note="N->C: Activation of HIV-1 Tat function."
FT /evidence="ECO:0000269|PubMed:10364329"
FT CONFLICT 682
FT /note="S -> C (in Ref. 1; AAC39666)"
FT /evidence="ECO:0000305"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 30..50
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:2IVX"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2IVX"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 79..93
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 123..142
FT /evidence="ECO:0007829|PDB:2IVX"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 167..183
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 230..245
FT /evidence="ECO:0007829|PDB:2IVX"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:2IVX"
SQ SEQUENCE 730 AA; 81029 MW; F449DFFC57FB196B CRC64;
MASGRGASSR WFFTREQLEN TPSRRCGVEA DKELSCRQQA ANLIQEMGQR LNVSQLTINT
AIVYMHRFYM HHSFTKFNKN IISSTALFLA AKVEEQARKL EHVIKVAHAC LHPLEPLLDT
KCDAYLQQTQ ELVILETIML QTLGFEITIE HPHTDVVKCT QLVRASKDLA QTSYFMATNS
LHLTTFCLQY KPTVIACVCI HLACKWSNWE IPVSTDGKHW WEYVDPTVTL ELLDELTHEF
LQILEKTPNR LKKIRNWRAN QAARKPKVDG QVSETPLLGS SLVQNSILVD SVTGVPTNPS
FQKPSTSAFP APVPLNSGNI SVQDSHTSDN LSMLATGMPS TSYGLSSHQE WPQHQDSART
EQLYSQKQET SLSGSQYNIN FQQGPSISLH SGLHHRPDKI SDHSSVKQEY THKAGSSKHH
GPISTTPGII PQKMSLDKYR EKRKLETLDL DVRDHYIAAQ VEQQHKQGQS QAASSSSVTS
PIKMKIPIAN TEKYMADKKE KSGSLKLRIP IPPTDKSASK EELKMKIKVS SSERHSSSDE
GSGKSKHSSP HISRDHKEKH KEHPSSRHHT SSHKHSHSHS GSSSGGSKHS ADGIPPTVLR
SPVGLSSDGI SSSSSSSRKR LHVNDASHNH HSKMSKSSKS SGSSSSSSSS VKQYISSHNS
VFNHPLPPPP PVTYQVGYGH LSTLVKLDKK PVETNGPDAN HEYSTSSQHM DYKDTFDMLD
SLLSAQGMNM
