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Protein

Kelch-like protein 42

Gene

KLHL42

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of KATNA1. Involved in microtubule dynamics throughout mitosis.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • regulation of microtubule-based process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Kelch-like protein 42
Alternative name(s):
Cullin-3-binding protein 9
Short name:
Ctb9
Kelch domain-containing protein 5
Gene namesi
Name:KLHL42
Synonyms:KIAA1340, KLHDC5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:29252. KLHL42.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeletonspindle 1 Publication

  • Note: Predominantly in mitotic cells. Localized diffusely in the cytoplasm during the interphase. During metaphase is localized throughout the cell and more widely dispersed than the microtubules. In anaphase cells is localized between the two sets of separated chromosomes as well as at the spindle poles. During telophase is localized arround the nuclei of the two daughter cells. Not detected at the midbody region during cytokinesis.

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671579.

Polymorphism and mutation databases

BioMutaiKLHL42.
DMDMi84028217.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Kelch-like protein 42PRO_0000119128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P2K6.
MaxQBiQ9P2K6.
PaxDbiQ9P2K6.
PeptideAtlasiQ9P2K6.
PRIDEiQ9P2K6.

PTM databases

iPTMnetiQ9P2K6.
PhosphoSiteiQ9P2K6.

Expressioni

Inductioni

Up-regulated during mitosis.1 Publication

Gene expression databases

BgeeiQ9P2K6.
CleanExiHS_KLHDC5.
ExpressionAtlasiQ9P2K6. baseline and differential.
GenevisibleiQ9P2K6. HS.

Organism-specific databases

HPAiHPA020979.

Interactioni

Subunit structurei

Component of the BCR(KLHL42) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL42. Interacts (via the BTB domain) with CUL3. Interacts (via the kelch domains) with KATNA1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCOCO2Q131373EBI-739890,EBI-739580
DDI1Q8WTU03EBI-739890,EBI-748248
FAM168AQ925673EBI-739890,EBI-7957930
SSX2IPQ9Y2D83EBI-739890,EBI-2212028
STAM2O758863EBI-739890,EBI-373258
STXBP4Q08AL93EBI-739890,EBI-10318905
TRIM23P364063EBI-739890,EBI-740098
UBQLN1Q9UMX0-23EBI-739890,EBI-10173939

Protein-protein interaction databases

BioGridi121601. 43 interactions.
IntActiQ9P2K6. 16 interactions.
MINTiMINT-2875160.
STRINGi9606.ENSP00000370671.

Structurei

3D structure databases

ProteinModelPortaliQ9P2K6.
SMRiQ9P2K6. Positions 218-488.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 7874BTBPROSITE-ProRule annotationAdd
BLAST
Repeati176 – 23459Kelch 1Add
BLAST
Repeati235 – 28248Kelch 2Add
BLAST
Repeati284 – 32542Kelch 3Add
BLAST
Repeati327 – 37246Kelch 4Add
BLAST
Repeati374 – 42956Kelch 5Add
BLAST
Repeati431 – 48050Kelch 6Add
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 6 Kelch repeats.Curated

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiKOG1072. Eukaryota.
ENOG4110X8D. LUCA.
GeneTreeiENSGT00760000118825.
HOGENOMiHOG000060089.
HOVERGENiHBG052263.
InParanoidiQ9P2K6.
OMAiTCTLHND.
OrthoDBiEOG757CX2.
PhylomeDBiQ9P2K6.
TreeFamiTF328485.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
InterProiIPR011705. BACK.
IPR000210. BTB/POZ_dom.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PfamiPF07707. BACK. 1 hit.
PF01344. Kelch_1. 2 hits.
[Graphical view]
SMARTiSM00612. Kelch. 3 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 2 hits.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P2K6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAEEMVQIR LEDRCYPVSK RKLIEQSDYF RALYRSGMRE ALSQEAGGPE
60 70 80 90 100
VQQLRGLSAP GLRLVLDFIN AGGAREGWLL GPRGEKGGGV DEDEEMDEVS
110 120 130 140 150
LLSELVEAAS FLQVTSLLQL LLSQVRLNNC LEMYRLAQVY GLPDLQEACL
160 170 180 190 200
RFMVVHFHEV LCKPQFHLLG SPPQAPGDVS LKQRLREARM TGTPVLVALG
210 220 230 240 250
DFLGGPLAPH PYQGEPPSML RYEEMTERWF PLANNLPPDL VNVRGYGSAI
260 270 280 290 300
LDNYLFIVGG YRITSQEISA AHSYNPSTNE WLQVASMNQK RSNFKLVAVN
310 320 330 340 350
SKLYAIGGQA VSNVECYNPE QDAWNFVAPL PNPLAEFSAC ECKGKIYVIG
360 370 380 390 400
GYTTRDRNMN ILQYCPSSDM WTLFETCDVH IRKQQMVSVE ETIYIVGGCL
410 420 430 440 450
HELGPNRRSS QSEDMLTVQS YNTVTRQWLY LKENTSKSGL NLTCALHNDG
460 470 480 490 500
IYIMSRDVTL STSLEHRVFL KYNIFSDSWE AFRRFPAFGH NLLVSSLYLP

NKAET
Length:505
Mass (Da):56,868
Last modified:December 20, 2005 - v2
Checksum:i999DF22ED3A546ED
GO

Sequence cautioni

The sequence AAH28742.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009511 Genomic DNA. No translation available.
BC108669 mRNA. Translation: AAI08670.1.
BC028742 mRNA. Translation: AAH28742.2. Different initiation.
AB037761 mRNA. Translation: BAA92578.1.
CCDSiCCDS31763.1.
RefSeqiNP_065833.1. NM_020782.1.
UniGeneiHs.505104.

Genome annotation databases

EnsembliENST00000381271; ENSP00000370671; ENSG00000087448.
GeneIDi57542.
KEGGihsa:57542.
UCSCiuc001rij.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009511 Genomic DNA. No translation available.
BC108669 mRNA. Translation: AAI08670.1.
BC028742 mRNA. Translation: AAH28742.2. Different initiation.
AB037761 mRNA. Translation: BAA92578.1.
CCDSiCCDS31763.1.
RefSeqiNP_065833.1. NM_020782.1.
UniGeneiHs.505104.

3D structure databases

ProteinModelPortaliQ9P2K6.
SMRiQ9P2K6. Positions 218-488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121601. 43 interactions.
IntActiQ9P2K6. 16 interactions.
MINTiMINT-2875160.
STRINGi9606.ENSP00000370671.

PTM databases

iPTMnetiQ9P2K6.
PhosphoSiteiQ9P2K6.

Polymorphism and mutation databases

BioMutaiKLHL42.
DMDMi84028217.

Proteomic databases

EPDiQ9P2K6.
MaxQBiQ9P2K6.
PaxDbiQ9P2K6.
PeptideAtlasiQ9P2K6.
PRIDEiQ9P2K6.

Protocols and materials databases

DNASUi57542.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381271; ENSP00000370671; ENSG00000087448.
GeneIDi57542.
KEGGihsa:57542.
UCSCiuc001rij.4. human.

Organism-specific databases

CTDi57542.
GeneCardsiKLHL42.
HGNCiHGNC:29252. KLHL42.
HPAiHPA020979.
neXtProtiNX_Q9P2K6.
PharmGKBiPA142671579.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1072. Eukaryota.
ENOG4110X8D. LUCA.
GeneTreeiENSGT00760000118825.
HOGENOMiHOG000060089.
HOVERGENiHBG052263.
InParanoidiQ9P2K6.
OMAiTCTLHND.
OrthoDBiEOG757CX2.
PhylomeDBiQ9P2K6.
TreeFamiTF328485.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GenomeRNAii57542.
PROiQ9P2K6.

Gene expression databases

BgeeiQ9P2K6.
CleanExiHS_KLHDC5.
ExpressionAtlasiQ9P2K6. baseline and differential.
GenevisibleiQ9P2K6. HS.

Family and domain databases

Gene3Di2.120.10.80. 1 hit.
InterProiIPR011705. BACK.
IPR000210. BTB/POZ_dom.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PfamiPF07707. BACK. 1 hit.
PF01344. Kelch_1. 2 hits.
[Graphical view]
SMARTiSM00612. Kelch. 3 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 2 hits.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Uterus.
  3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-505.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  5. "The Cul3/Klhdc5 E3 ligase regulates p60/katanin and is required for normal mitosis in mammalian cells."
    Cummings C.M., Bentley C.A., Perdue S.A., Baas P.W., Singer J.D.
    J. Biol. Chem. 284:11663-11675(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BCR(KLHL42) COMPLEX, FUNCTION, INTERACTION WITH CUL3 AND KATNA1, INDUCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiKLH42_HUMAN
AccessioniPrimary (citable) accession number: Q9P2K6
Secondary accession number(s): Q2VPK1, Q8N334
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: December 20, 2005
Last modified: July 6, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.