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   27-MAR-2024, entry version 172.
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   -!- INTERACTION:
CC       Q9P2J3; Q96GD4: AURKB; NbExp=2; IntAct=EBI-2510152, EBI-624291;
CC       Q9P2J3; Q13618: CUL3; NbExp=12; IntAct=EBI-2510152, EBI-456129;
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; 121.
DR   ComplexPortal; CPX-8083; CRL3 E3 ubiquitin ligase complex, KLHL9 variant.
DR   CORUM; Q9P2J3; -.
DR   DIP; DIP-53514N; -.
DR   IntAct; Q9P2J3; 22.
DR   MINT; Q9P2J3; -.
DR   STRING; 9606.ENSP00000351933; -.
DR   GlyGen; Q9P2J3; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000351933; -.
DR   PeptideAtlas; Q9P2J3; -.
DR   ProteomicsDB; 83821; -.
DR   Pumba; Q9P2J3; -.
DR   Antibodypedia; 24868; 179 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   AGR; HGNC:18732; -.
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; 5472491at2759; -.
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   SIGNOR; Q9P2J3; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 55958; 17 hits in 1191 CRISPR screens.
DR   ChiTaRS; KLHL9; human.
DR   GenomeRNAi; 55958; -.
DR   Pharos; Q9P2J3; Tbio.
DR   PRO; PR:Q9P2J3; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9P2J3; Protein.
DR   Bgee; ENSG00000198642; Expressed in corpus epididymis and 212 other cell types or tissues.
DR   ExpressionAtlas; Q9P2J3; baseline and differential.
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   CDD; cd18449; BACK_KLHL9_13; 1.
DR   CDD; cd18239; BTB_POZ_KLHL9_13; 1.
DR   Gene3D; 1.25.40.420; -; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 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   PANTHER; PTHR45632:SF11; KELCH-LIKE PROTEIN 9; 1.
DR   PANTHER; PTHR45632; LD33804P; 1.
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; Kelch motif; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   Genevisible; Q9P2J3; HS.
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
//