CCH11_ARATH
ID CCH11_ARATH Reviewed; 336 AA.
AC Q8W5S1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Cyclin-H1-1;
DE Short=CycH1;1;
GN Name=CYCH1-1; Synonyms=CYCH1; OrderedLocusNames=At5g27620;
GN ORFNames=F15A18.80;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CDKA-1; CDKD-2
RP AND CDKD-3.
RX PubMed=15486101; DOI=10.1105/tpc.104.025601;
RA Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M.;
RT "The plant-specific kinase CDKF;1 is involved in activating phosphorylation
RT of cyclin-dependent kinase-activating kinases in Arabidopsis.";
RL Plant Cell 16:2954-2966(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15208425; DOI=10.1104/pp.104.040436;
RA Wang G., Kong H., Sun Y., Zhang X., Zhang W., Altman N., dePamphilis C.W.,
RA Ma H.;
RT "Genome-wide analysis of the cyclin family in Arabidopsis and comparative
RT phylogenetic analysis of plant cyclin-like proteins.";
RL Plant Physiol. 135:1084-1099(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDKD-2 AND CDKD-3.
RC STRAIN=cv. Columbia;
RX PubMed=16856985; DOI=10.1111/j.1365-313x.2006.02820.x;
RA Shimotohno A., Ohno R., Bisova K., Sakaguchi N., Huang J., Koncz C.,
RA Uchimiya H., Umeda M.;
RT "Diverse phosphoregulatory mechanisms controlling cyclin-dependent kinase-
RT activating kinases in Arabidopsis.";
RL Plant J. 47:701-710(2006).
RN [7]
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).
CC -!- FUNCTION: Associates with CDK-2 and CDK-3 and activates the CDK
CC kinases. {ECO:0000269|PubMed:15486101}.
CC -!- SUBUNIT: Interacts with CDKA-1, CDKD-2 and CDKD-3, but not CDKD-1 and
CC CDKF-1. {ECO:0000269|PubMed:15486101, ECO:0000269|PubMed:16856985}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16856985}. Nucleus
CC {ECO:0000269|PubMed:16856985}.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR EMBL; AB051072; BAB72144.1; -; mRNA.
DR EMBL; AC007478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93707.1; -; Genomic_DNA.
DR EMBL; AK118707; BAC43301.1; -; mRNA.
DR RefSeq; NP_198114.2; NM_122644.5.
DR AlphaFoldDB; Q8W5S1; -.
DR SMR; Q8W5S1; -.
DR BioGRID; 18098; 42.
DR IntAct; Q8W5S1; 23.
DR STRING; 3702.AT5G27620.1; -.
DR iPTMnet; Q8W5S1; -.
DR PaxDb; Q8W5S1; -.
DR PRIDE; Q8W5S1; -.
DR EnsemblPlants; AT5G27620.1; AT5G27620.1; AT5G27620.
DR GeneID; 832824; -.
DR Gramene; AT5G27620.1; AT5G27620.1; AT5G27620.
DR KEGG; ath:AT5G27620; -.
DR Araport; AT5G27620; -.
DR TAIR; locus:2143671; AT5G27620.
DR eggNOG; KOG2496; Eukaryota.
DR HOGENOM; CLU_022620_1_1_1; -.
DR InParanoid; Q8W5S1; -.
DR OMA; FRVEQNT; -.
DR PhylomeDB; Q8W5S1; -.
DR PRO; PR:Q8W5S1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W5S1; baseline and differential.
DR Genevisible; Q8W5S1; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:2000070; P:regulation of response to water deprivation; IMP:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEP:TAIR.
DR GO; GO:0009637; P:response to blue light; IMP:CACAO.
DR GO; GO:0009414; P:response to water deprivation; IMP:CACAO.
DR GO; GO:1990069; P:stomatal opening; IMP:TAIR.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR031658; Cyclin_C_2.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR Pfam; PF16899; Cyclin_C_2; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cyclin; Cytoplasm; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..336
FT /note="Cyclin-H1-1"
FT /id="PRO_0000287049"
FT REGION 297..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
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"
SQ SEQUENCE 336 AA; 38131 MW; 488BCDA2B9B58C1A CRC64;
MADFQTSTQR AKWIFTPQKL AERYKAANQR AVQMLEKCGT TQVEVDASGS LTYPKDKVGS
GDQADKKLKP LSADEERFMR AFYEAKVQEV CSAFAFPHKI QATALQYFKR FYLQWSVMQH
HPKEIMLTCV YAACKIEENH VSAEEIGKGI NQDHRIILKY EMAVLQSLEF DLIVYAPYRA
IEGFVNNMEE FLQARDDEIQ KLESLLKGAT AEADKVMLTD APLLFPPGQL ALASLRIANG
VLGVIDFDRY LENIVSQPNS EHTTSELTKL LDNIEYLVKN YKCPSEKDMK HINRKLKSCL
GHSSSHDESK KREKRSKHKS HRSSNDTPNG APPPIG
