CCNQ_HUMAN
ID CCNQ_HUMAN Reviewed; 248 AA.
AC Q8N1B3; Q2I380; Q330J9; Q96IU5; Q9BUU1;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cyclin-Q;
DE AltName: Full=CDK10-activating cyclin;
DE AltName: Full=Cyclin-M;
DE AltName: Full=Cyclin-related protein FAM58A;
GN Name=CCNQ {ECO:0000312|HGNC:HGNC:28434}; Synonyms=FAM58A;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-183.
RC TISSUE=B-cell, Blood, Kidney, and Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-228 (ISOFORM 2).
RA Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Liang M., Tang Z.,
RA Huang B., Li H., Yang S.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-130 (ISOFORM 1).
RA Johne C., Tschop K., Engeland K.;
RT "Cyclin M.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, INTERACTION WITH SALL1, AND INVOLVEMENT IN STAR.
RX PubMed=18297069; DOI=10.1038/ng.86;
RA Unger S., Boehm D., Kaiser F.J., Kaulfuss S., Borozdin W., Buiting K.,
RA Burfeind P., Boehm J., Barrionuevo F., Craig A., Borowski K.,
RA Keppler-Noreuil K., Schmitt-Mechelke T., Steiner B., Bartholdi D.,
RA Lemke J., Mortier G., Sandford R., Zabel B., Superti-Furga A., Kohlhase J.;
RT "Mutations in the cyclin family member FAM58A cause an X-linked dominant
RT disorder characterized by syndactyly, telecanthus and anogenital and renal
RT malformations.";
RL Nat. Genet. 40:287-289(2008).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [7]
RP FUNCTION, MISCELLANEOUS, AND INTERACTION WITH CDK10.
RX PubMed=24218572; DOI=10.1073/pnas.1306814110;
RA Guen V.J., Gamble C., Flajolet M., Unger S., Thollet A., Ferandin Y.,
RA Superti-Furga A., Cohen P.A., Meijer L., Colas P.;
RT "CDK10/cyclin M is a protein kinase that controls ETS2 degradation and is
RT deficient in STAR syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19525-19530(2013).
CC -!- FUNCTION: Activating cyclin for the cyclin-associated kinase CDK10.
CC {ECO:0000269|PubMed:18297069, ECO:0000269|PubMed:24218572}.
CC -!- SUBUNIT: Associates with CDK10 to promote its kinase activity.
CC Interacts with SALL1. {ECO:0000269|PubMed:18297069,
CC ECO:0000269|PubMed:24218572}.
CC -!- INTERACTION:
CC Q8N1B3; Q15131-1: CDK10; NbExp=7; IntAct=EBI-3925043, EBI-11507283;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N1B3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N1B3-2; Sequence=VSP_034527;
CC -!- DISEASE: Toe syndactyly, telecanthus, and anogenital and renal
CC malformations (STAR) [MIM:300707]: A syndrome characterized by anal,
CC genital and renal tract anomalies, facial dysmorphism and syndactyly.
CC Features include anal stenosis, a rectovaginal fistula, clitoral
CC hypertrophy, a pelvic right kidney, toe syndactyly, and telecanthus.
CC {ECO:0000269|PubMed:18297069}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Silencing with siRNAs phenocopies CDK10 silencing in
CC increasing c-Raf and in conferring tamoxifen resistance to breast
CC cancer cells.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin-like FAM58 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01909.4; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH07232.4; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH32121.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH71851.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC001909; AAH01909.4; ALT_INIT; mRNA.
DR EMBL; BC007232; AAH07232.4; ALT_INIT; mRNA.
DR EMBL; BC032121; AAH32121.1; ALT_INIT; mRNA.
DR EMBL; BC071851; AAH71851.1; ALT_INIT; mRNA.
DR EMBL; DQ323993; ABC88595.1; -; mRNA.
DR EMBL; AY445048; AAS20614.1; -; mRNA.
DR CCDS; CCDS76054.1; -. [Q8N1B3-2]
DR RefSeq; NP_001124469.1; NM_001130997.2. [Q8N1B3-2]
DR RefSeq; NP_689487.2; NM_152274.4. [Q8N1B3-1]
DR AlphaFoldDB; Q8N1B3; -.
DR SMR; Q8N1B3; -.
DR BioGRID; 124901; 19.
DR ComplexPortal; CPX-326; Cyclin M-CDK10 complex.
DR IntAct; Q8N1B3; 16.
DR MINT; Q8N1B3; -.
DR STRING; 9606.ENSP00000402949; -.
DR iPTMnet; Q8N1B3; -.
DR PhosphoSitePlus; Q8N1B3; -.
DR BioMuta; CCNQ; -.
DR DMDM; 156630447; -.
DR EPD; Q8N1B3; -.
DR jPOST; Q8N1B3; -.
DR MassIVE; Q8N1B3; -.
DR MaxQB; Q8N1B3; -.
DR PaxDb; Q8N1B3; -.
DR PeptideAtlas; Q8N1B3; -.
DR PRIDE; Q8N1B3; -.
DR ProteomicsDB; 71580; -. [Q8N1B3-1]
DR ProteomicsDB; 71581; -. [Q8N1B3-2]
DR Antibodypedia; 73523; 29 antibodies from 12 providers.
DR DNASU; 92002; -.
DR Ensembl; ENST00000440428.5; ENSP00000402949.2; ENSG00000262919.8. [Q8N1B3-2]
DR Ensembl; ENST00000576892.8; ENSP00000461135.1; ENSG00000262919.8. [Q8N1B3-1]
DR GeneID; 92002; -.
DR KEGG; hsa:92002; -.
DR MANE-Select; ENST00000576892.8; ENSP00000461135.1; NM_152274.5; NP_689487.2.
DR UCSC; uc033fat.2; human. [Q8N1B3-1]
DR CTD; 92002; -.
DR DisGeNET; 92002; -.
DR GeneCards; CCNQ; -.
DR HGNC; HGNC:28434; CCNQ.
DR HPA; ENSG00000262919; Low tissue specificity.
DR MalaCards; CCNQ; -.
DR MIM; 300707; phenotype.
DR MIM; 300708; gene.
DR neXtProt; NX_Q8N1B3; -.
DR OpenTargets; ENSG00000262919; -.
DR Orphanet; 140952; Syndactyly-telecanthus-anogenital and renal malformations syndrome.
DR PharmGKB; PA142671863; -.
DR VEuPathDB; HostDB:ENSG00000262919; -.
DR eggNOG; KOG0834; Eukaryota.
DR GeneTree; ENSGT00940000155445; -.
DR HOGENOM; CLU_022000_2_0_1; -.
DR InParanoid; Q8N1B3; -.
DR OMA; FDTHVAL; -.
DR OrthoDB; 958680at2759; -.
DR PhylomeDB; Q8N1B3; -.
DR PathwayCommons; Q8N1B3; -.
DR SignaLink; Q8N1B3; -.
DR BioGRID-ORCS; 92002; 24 hits in 179 CRISPR screens.
DR ChiTaRS; FAM58A; human.
DR GenomeRNAi; 92002; -.
DR Pharos; Q8N1B3; Tdark.
DR PRO; PR:Q8N1B3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8N1B3; protein.
DR Bgee; ENSG00000262919; Expressed in tendon of biceps brachii and 180 other tissues.
DR ExpressionAtlas; Q8N1B3; baseline and differential.
DR Genevisible; Q8N1B3; HS.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR028759; Cyclin-Q.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR PANTHER; PTHR10026:SF70; PTHR10026:SF70; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cyclin; Reference proteome.
FT CHAIN 1..248
FT /note="Cyclin-Q"
FT /id="PRO_0000297567"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT VAR_SEQ 219..238
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034527"
FT VARIANT 183
FT /note="C -> S (in dbSNP:rs17850173)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034642"
SQ SEQUENCE 248 AA; 28369 MW; E7C11BC5D23BFB82 CRC64;
MEAPEGGGGG PAARGPEGQP APEARVHFRV ARFIMEAGVK LGMRSIPIAT ACTIYHKFFC
ETNLDAYDPY LIAMSSIYLA GKVEEQHLRT RDIINVSNRY FNPSGEPLEL DSRFWELRDS
IVQCELLMLR VLRFQVSFQH PHKYLLHYLV SLQNWLNRHS WQRTPVAVTA WALLRDSYHG
ALCLRFQAQH IAVAVLYLAL QVYGVEVPAE VEAEKPWWQV FNDDLTKPII DNIVSDLIQI
YTMDTEIP
