KLHL9_HUMAN
ID KLHL9_HUMAN Reviewed; 617 AA.
AC Q9P2J3; Q8TCQ2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Kelch-like protein 9;
GN Name=KLHL9; Synonyms=KIAA1354;
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].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH CUL3.
RX PubMed=14528312; DOI=10.1038/ncb1056;
RA Furukawa M., He Y.J., Borchers C., Xiong Y.;
RT "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
RT ligases.";
RL Nat. Cell Biol. 5:1001-1007(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH AURKB; CUL3 AND KLHL13.
RX PubMed=17543862; DOI=10.1016/j.devcel.2007.03.019;
RA Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., Peter M.;
RT "A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes,
RT regulating mitotic progression and completion of cytokinesis in human
RT cells.";
RL Dev. Cell 12:887-900(2007).
RN [5]
RP FUNCTION.
RX PubMed=19995937; DOI=10.1083/jcb.200906117;
RA Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W., Quadroni M.,
RA Sumara I., Peter M.;
RT "The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone
RT microtubules in anaphase and is required for cytokinesis.";
RL J. Cell Biol. 187:791-800(2009).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex required for mitotic progression and
CC cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex mediates
CC the ubiquitination of AURKB and controls the dynamic behavior of AURKB
CC on mitotic chromosomes and thereby coordinates faithful mitotic
CC progression and completion of cytokinesis.
CC {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17543862,
CC ECO:0000269|PubMed:19995937}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(KLHL9-KLHL13) E3 ubiquitin ligase
CC complex, at least composed of CUL3, KLHL9, KLHL13 and RBX1. Interacts
CC with AURKB. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:17543862}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92592.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB037775; BAA92592.1; ALT_INIT; mRNA.
DR EMBL; AL713669; CAD28475.1; -; mRNA.
DR CCDS; CCDS6503.1; -.
DR RefSeq; NP_061335.1; NM_018847.3.
DR AlphaFoldDB; Q9P2J3; -.
DR SMR; Q9P2J3; -.
DR BioGRID; 121009; 120.
DR CORUM; Q9P2J3; -.
DR DIP; DIP-53514N; -.
DR IntAct; Q9P2J3; 14.
DR STRING; 9606.ENSP00000351933; -.
DR iPTMnet; Q9P2J3; -.
DR PhosphoSitePlus; Q9P2J3; -.
DR BioMuta; KLHL9; -.
DR DMDM; 51338828; -.
DR EPD; Q9P2J3; -.
DR jPOST; Q9P2J3; -.
DR MassIVE; Q9P2J3; -.
DR MaxQB; Q9P2J3; -.
DR PaxDb; Q9P2J3; -.
DR PeptideAtlas; Q9P2J3; -.
DR PRIDE; Q9P2J3; -.
DR ProteomicsDB; 83821; -.
DR Antibodypedia; 24868; 156 antibodies from 24 providers.
DR DNASU; 55958; -.
DR Ensembl; ENST00000359039.5; ENSP00000351933.4; ENSG00000198642.7.
DR GeneID; 55958; -.
DR KEGG; hsa:55958; -.
DR MANE-Select; ENST00000359039.5; ENSP00000351933.4; NM_018847.4; NP_061335.1.
DR UCSC; uc003zoy.4; human.
DR CTD; 55958; -.
DR DisGeNET; 55958; -.
DR GeneCards; KLHL9; -.
DR HGNC; HGNC:18732; KLHL9.
DR HPA; ENSG00000198642; Low tissue specificity.
DR MalaCards; KLHL9; -.
DR MIM; 611201; gene.
DR neXtProt; NX_Q9P2J3; -.
DR OpenTargets; ENSG00000198642; -.
DR Orphanet; 399081; KLHL9-related early-onset distal myopathy.
DR PharmGKB; PA38662; -.
DR VEuPathDB; HostDB:ENSG00000198642; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000154359; -.
DR HOGENOM; CLU_004253_14_3_1; -.
DR InParanoid; Q9P2J3; -.
DR OMA; RAQEWKS; -.
DR OrthoDB; 250404at2759; -.
DR PhylomeDB; Q9P2J3; -.
DR TreeFam; TF328485; -.
DR PathwayCommons; Q9P2J3; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9P2J3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55958; 17 hits in 1113 CRISPR screens.
DR ChiTaRS; KLHL9; human.
DR GenomeRNAi; 55958; -.
DR Pharos; Q9P2J3; Tdark.
DR PRO; PR:Q9P2J3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9P2J3; protein.
DR Bgee; ENSG00000198642; Expressed in corpus epididymis and 210 other tissues.
DR ExpressionAtlas; Q9P2J3; baseline and differential.
DR Genevisible; Q9P2J3; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0097602; F:cullin family protein 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:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 5.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Kelch repeat; Mitosis; Reference proteome;
KW Repeat; Ubl conjugation pathway.
FT CHAIN 1..617
FT /note="Kelch-like protein 9"
FT /id="PRO_0000119110"
FT DOMAIN 50..119
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 154..255
FT /note="BACK"
FT REPEAT 300..347
FT /note="Kelch 1"
FT REPEAT 348..399
FT /note="Kelch 2"
FT REPEAT 400..446
FT /note="Kelch 3"
FT REPEAT 448..493
FT /note="Kelch 4"
FT REPEAT 495..545
FT /note="Kelch 5"
FT REPEAT 546..595
FT /note="Kelch 6"
FT REGION 595..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 69429 MW; B74232F28ABF7C82 CRC64;
MKVSLGNGEM GVSAHLQPCK AGTTRFFTSN THSSVVLQGF DQLRIEGLLC DVTLVPGDGD
EIFPVHRAMM ASASDYFKAM FTGGMKEQDL MCIKLHGVNK VGLKKIIDFI YTAKLSLNMD
NLQDTLEAAS FLQILPVLDF CKVFLISGVS LDNCVEVGRI ANTYNLIEVD KYVNNFILKN
FPALLSTGEF LKLPFERLAF VLSSNSLKHC TELELFKAAC RWLRLEDPRM DYAAKLMKNI
RFPLMTPQDL INYVQTVDFM RTDNTCVNLL LEASNYQMMP YMQPVMQSDR TAIRSDSTHL
VTLGGVLRQQ LVVSKELRMY DERAQEWRSL APMDAPRYQH GIAVIGNFLY VVGGQSNYDT
KGKTAVDTVF RFDPRYNKWM QVASLNEKRT FFHLSALKGH LYAVGGRSAA GELATVECYN
PRMNEWSYVA KMSEPHYGHA GTVYGGLMYI SGGITHDTFQ NELMCFDPDT DKWMQKAPMT
TVRGLHCMCT VGDKLYVIGG NHFRGTSDYD DVLSCEYYSP TLDQWTPIAA MLRGQSDVGV
AVFENKIYVV GGYSWNNRCM VEIVQKYDPE KDEWHKVFDL PESLGGIRAC TLTVFPPEEN
PGSPSRESPL SAPSDHS
