KLH42_HUMAN
ID KLH42_HUMAN Reviewed; 505 AA.
AC Q9P2K6; Q2VPK1; Q8N334;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Kelch-like protein 42;
DE AltName: Full=Cullin-3-binding protein 9;
DE Short=Ctb9;
DE AltName: Full=Kelch domain-containing protein 5;
GN Name=KLHL42; Synonyms=KIAA1340, KLHDC5;
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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-505.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP IDENTIFICATION IN THE BCR(KLHL42) COMPLEX, FUNCTION, INTERACTION WITH CUL3
RP AND KATNA1, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19261606; DOI=10.1074/jbc.m809374200;
RA Cummings C.M., Bentley C.A., Perdue S.A., Baas P.W., Singer J.D.;
RT "The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for normal
RT mitosis in mammalian cells.";
RL J. Biol. Chem. 284:11663-11675(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(KLHL42) E3 ubiquitin ligase complex mediates the
CC ubiquitination and subsequent degradation of KATNA1. Involved in
CC microtubule dynamics throughout mitosis. {ECO:0000269|PubMed:19261606}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the BCR(KLHL42) E3 ubiquitin ligase complex, at
CC least composed of CUL3 and KLHL42. Interacts (via the BTB domain) with
CC CUL3. Interacts (via the kelch domains) with KATNA1.
CC {ECO:0000269|PubMed:19261606}.
CC -!- INTERACTION:
CC Q9P2K6; Q96D30: ADD1; NbExp=3; IntAct=EBI-739890, EBI-9089447;
CC Q9P2K6; Q7Z3H0-1: ANKRD33; NbExp=3; IntAct=EBI-739890, EBI-16746154;
CC Q9P2K6; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-739890, EBI-739580;
CC Q9P2K6; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-739890, EBI-1773949;
CC Q9P2K6; P17540: CKMT2; NbExp=3; IntAct=EBI-739890, EBI-712973;
CC Q9P2K6; Q8WUE5: CT55; NbExp=3; IntAct=EBI-739890, EBI-6873363;
CC Q9P2K6; Q15038: DAZAP2; NbExp=3; IntAct=EBI-739890, EBI-724310;
CC Q9P2K6; Q8WTU0: DDI1; NbExp=8; IntAct=EBI-739890, EBI-748248;
CC Q9P2K6; Q92567: FAM168A; NbExp=3; IntAct=EBI-739890, EBI-7957930;
CC Q9P2K6; Q0VD86: INCA1; NbExp=3; IntAct=EBI-739890, EBI-6509505;
CC Q9P2K6; Q3LI73: KRTAP19-4; NbExp=3; IntAct=EBI-739890, EBI-12958461;
CC Q9P2K6; P15173: MYOG; NbExp=3; IntAct=EBI-739890, EBI-3906629;
CC Q9P2K6; O43482: OIP5; NbExp=3; IntAct=EBI-739890, EBI-536879;
CC Q9P2K6; P07237: P4HB; NbExp=3; IntAct=EBI-739890, EBI-395883;
CC Q9P2K6; Q99471: PFDN5; NbExp=3; IntAct=EBI-739890, EBI-357275;
CC Q9P2K6; P01189: POMC; NbExp=3; IntAct=EBI-739890, EBI-12219503;
CC Q9P2K6; Q04864-2: REL; NbExp=3; IntAct=EBI-739890, EBI-10829018;
CC Q9P2K6; Q9UHV2: SERTAD1; NbExp=4; IntAct=EBI-739890, EBI-748601;
CC Q9P2K6; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-739890, EBI-748621;
CC Q9P2K6; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-739890, EBI-2212028;
CC Q9P2K6; O75886: STAM2; NbExp=6; IntAct=EBI-739890, EBI-373258;
CC Q9P2K6; Q08AL9: STXBP4; NbExp=3; IntAct=EBI-739890, EBI-10318905;
CC Q9P2K6; P36406: TRIM23; NbExp=6; IntAct=EBI-739890, EBI-740098;
CC Q9P2K6; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-739890, EBI-2130429;
CC Q9P2K6; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-739890, EBI-9090990;
CC Q9P2K6; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-739890, EBI-741480;
CC Q9P2K6; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-739890, EBI-10173939;
CC Q9P2K6; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-739890, EBI-947187;
CC Q9P2K6; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-739890, EBI-2799833;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19261606}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19261606}.
CC Note=Predominantly in mitotic cells. Localized diffusely in the
CC cytoplasm during the interphase. During metaphase is localized
CC throughout the cell and more widely dispersed than the microtubules. In
CC anaphase cells is localized between the two sets of separated
CC chromosomes as well as at the spindle poles. During telophase is
CC localized arround the nuclei of the two daughter cells. Not detected at
CC the midbody region during cytokinesis.
CC -!- INDUCTION: Up-regulated during mitosis. {ECO:0000269|PubMed:19261606}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH28742.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108669; AAI08670.1; -; mRNA.
DR EMBL; BC028742; AAH28742.2; ALT_INIT; mRNA.
DR EMBL; AB037761; BAA92578.1; -; mRNA.
DR CCDS; CCDS31763.1; -.
DR RefSeq; NP_065833.1; NM_020782.1.
DR AlphaFoldDB; Q9P2K6; -.
DR SMR; Q9P2K6; -.
DR BioGRID; 121601; 92.
DR CORUM; Q9P2K6; -.
DR IntAct; Q9P2K6; 58.
DR STRING; 9606.ENSP00000370671; -.
DR GlyGen; Q9P2K6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P2K6; -.
DR PhosphoSitePlus; Q9P2K6; -.
DR BioMuta; KLHL42; -.
DR DMDM; 84028217; -.
DR EPD; Q9P2K6; -.
DR jPOST; Q9P2K6; -.
DR MassIVE; Q9P2K6; -.
DR MaxQB; Q9P2K6; -.
DR PaxDb; Q9P2K6; -.
DR PeptideAtlas; Q9P2K6; -.
DR PRIDE; Q9P2K6; -.
DR ProteomicsDB; 83837; -.
DR Antibodypedia; 12736; 128 antibodies from 26 providers.
DR DNASU; 57542; -.
DR Ensembl; ENST00000381271.7; ENSP00000370671.2; ENSG00000087448.11.
DR GeneID; 57542; -.
DR KEGG; hsa:57542; -.
DR MANE-Select; ENST00000381271.7; ENSP00000370671.2; NM_020782.2; NP_065833.1.
DR UCSC; uc001rij.4; human.
DR CTD; 57542; -.
DR DisGeNET; 57542; -.
DR GeneCards; KLHL42; -.
DR HGNC; HGNC:29252; KLHL42.
DR HPA; ENSG00000087448; Low tissue specificity.
DR MIM; 618919; gene.
DR neXtProt; NX_Q9P2K6; -.
DR OpenTargets; ENSG00000087448; -.
DR PharmGKB; PA142671579; -.
DR VEuPathDB; HostDB:ENSG00000087448; -.
DR eggNOG; KOG1072; Eukaryota.
DR GeneTree; ENSGT00940000160124; -.
DR HOGENOM; CLU_021248_1_0_1; -.
DR InParanoid; Q9P2K6; -.
DR OMA; LKYMSCH; -.
DR OrthoDB; 909276at2759; -.
DR PhylomeDB; Q9P2K6; -.
DR TreeFam; TF328485; -.
DR PathwayCommons; Q9P2K6; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9P2K6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 57542; 19 hits in 1120 CRISPR screens.
DR ChiTaRS; KLHL42; human.
DR GenomeRNAi; 57542; -.
DR Pharos; Q9P2K6; Tdark.
DR PRO; PR:Q9P2K6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9P2K6; protein.
DR Bgee; ENSG00000087448; Expressed in endothelial cell and 187 other tissues.
DR ExpressionAtlas; Q9P2K6; baseline and differential.
DR Genevisible; Q9P2K6; HS.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
DR CDD; cd18478; BACK_KLHL42_KLHDC5; 1.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR044727; KLHL42_BACK.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF01344; Kelch_1; 2.
DR SMART; SM00612; Kelch; 3.
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; Cytoplasm; Cytoskeleton; Kelch repeat; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..505
FT /note="Kelch-like protein 42"
FT /id="PRO_0000119128"
FT DOMAIN 5..78
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 176..234
FT /note="Kelch 1"
FT REPEAT 235..282
FT /note="Kelch 2"
FT REPEAT 284..325
FT /note="Kelch 3"
FT REPEAT 327..372
FT /note="Kelch 4"
FT REPEAT 374..429
FT /note="Kelch 5"
FT REPEAT 431..480
FT /note="Kelch 6"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
SQ SEQUENCE 505 AA; 56868 MW; 999DF22ED3A546ED CRC64;
MSAEEMVQIR LEDRCYPVSK RKLIEQSDYF RALYRSGMRE ALSQEAGGPE VQQLRGLSAP
GLRLVLDFIN AGGAREGWLL GPRGEKGGGV DEDEEMDEVS LLSELVEAAS FLQVTSLLQL
LLSQVRLNNC LEMYRLAQVY GLPDLQEACL RFMVVHFHEV LCKPQFHLLG SPPQAPGDVS
LKQRLREARM TGTPVLVALG DFLGGPLAPH PYQGEPPSML RYEEMTERWF PLANNLPPDL
VNVRGYGSAI LDNYLFIVGG YRITSQEISA AHSYNPSTNE WLQVASMNQK RSNFKLVAVN
SKLYAIGGQA VSNVECYNPE QDAWNFVAPL PNPLAEFSAC ECKGKIYVIG GYTTRDRNMN
ILQYCPSSDM WTLFETCDVH IRKQQMVSVE ETIYIVGGCL HELGPNRRSS QSEDMLTVQS
YNTVTRQWLY LKENTSKSGL NLTCALHNDG IYIMSRDVTL STSLEHRVFL KYNIFSDSWE
AFRRFPAFGH NLLVSSLYLP NKAET
