Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UJP4

- KLH21_HUMAN

UniProt

Q9UJP4 - KLH21_HUMAN

Protein

Kelch-like protein 21

Gene

KLHL21

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 4 (18 Mar 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome.2 Publications

    Pathwayi

    GO - Biological processi

    1. chromosome passenger complex localization to spindle midzone Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. protein ubiquitination Source: UniProtKB
    4. regulation of cytokinesis Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kelch-like protein 21
    Gene namesi
    Name:KLHL21
    Synonyms:KIAA0469
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29041. KLHL21.

    Subcellular locationi

    Cytoplasmcytoskeletonspindle 1 Publication
    Note: Localizes to the spindle midzone and targets CUL3 to this region.

    GO - Cellular componenti

    1. Cul3-RING ubiquitin ligase complex Source: UniProtKB
    2. cytoplasm Source: UniProtKB-KW
    3. polar microtubule Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1174DLLQ → AALA: Abolishes interaction with CUL3. 1 Publication

    Organism-specific databases

    PharmGKBiPA134989246.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 597597Kelch-like protein 21PRO_0000119125Add
    BLAST

    Proteomic databases

    MaxQBiQ9UJP4.
    PaxDbiQ9UJP4.
    PRIDEiQ9UJP4.

    PTM databases

    PhosphoSiteiQ9UJP4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UJP4.
    BgeeiQ9UJP4.
    CleanExiHS_KLHL21.
    GenevestigatoriQ9UJP4.

    Organism-specific databases

    HPAiHPA051364.

    Interactioni

    Subunit structurei

    Component of the BCR(KLHL21) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL21 and RBX1.1 Publication

    Protein-protein interaction databases

    BioGridi115232. 8 interactions.
    STRINGi9606.ENSP00000366886.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJP4.
    SMRiQ9UJP4. Positions 12-570.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 10369BTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini138 – 239102BACKAdd
    BLAST
    Repeati287 – 33549Kelch 1Add
    BLAST
    Repeati336 – 38247Kelch 2Add
    BLAST
    Repeati384 – 42239Kelch 3Add
    BLAST
    Repeati423 – 47048Kelch 4Add
    BLAST
    Repeati472 – 51241Kelch 5Add
    BLAST
    Repeati513 – 56048Kelch 6Add
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Kelch repeat, Repeat

    Phylogenomic databases

    eggNOGiNOG264826.
    HOGENOMiHOG000261671.
    HOVERGENiHBG101644.
    InParanoidiQ9UJP4.
    KOiK10458.
    OMAiWVRADPP.
    OrthoDBiEOG7WHH8X.
    PhylomeDBiQ9UJP4.
    TreeFamiTF329218.

    Family and domain databases

    Gene3Di2.130.10.80. 1 hit.
    3.30.710.10. 1 hit.
    InterProiIPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view]
    PfamiPF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 3 hits.
    [Graphical view]
    PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTiSM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 5 hits.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    PROSITEiPS50097. BTB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UJP4-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MERPAPLAVL PFSDPAHALS LLRGLSQLRA ERKFLDVTLE AAGGRDFPAH    50
    RAVLAAASPY FRAMFAGQLR ESRAERVRLH GVPPDMLQLL LDFSYTGRVA 100
    VSGDNAEPLL RAADLLQFPA VKEACGAFLQ QQLDLANCLD MQDFAEAFSC 150
    SGLASAAQRF ILRHVGELGA EQLERLPLAR LLRYLRDDGL CVPKEEAAYQ 200
    LALRWVRADP PRRAAHWPQL LEAVRLPFVR RFYLLAHVEA EPLVARCPPC 250
    LRLLREARDF QAARYDRHDR GPCPRMRPRP STGLAEILVL VGGCDQDCDE 300
    LVTVDCYNPQ TGQWRYLAEF PDHLGGGYSI VALGNDIYVT GGSDGSRLYD 350
    CVWRYNSSVN EWAEVAPMLK AREYHSSSVL DGLLYVVAAD STERYDHTTD 400
    SWEALQPMTY PMDNCSTTAC RGRLYAIGSL AGKETMVMQC YDPDTDLWSL 450
    VDCGQLPPWS FAPKTATLNG LMYFVRDDSA EVDVYNPTRN EWDKIPSMNQ 500
    VHVGGSLAVL GGKLYVSGGY DNTFELSDVV EAYDPETRAW SVVGRLPEPT 550
    FWHGSVSIFR QFMPQTFSGG RGFELDSGSD DMDPGRPRPP RDPDELH 597
    Length:597
    Mass (Da):66,617
    Last modified:March 18, 2008 - v4
    Checksum:iD3E682609F284645
    GO
    Isoform 2 (identifier: Q9UJP4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         502-539: HVGGSLAVLG...VEAYDPETRA → NFQAGQHWKH...TAMMGGSHLN
         540-597: Missing.

    Show »
    Length:539
    Mass (Da):60,378
    Checksum:iDDE88D184C05A945
    GO

    Sequence cautioni

    The sequence BAA32314.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti183 – 1831R → C in BAC03453. 1 PublicationCurated
    Sequence conflicti380 – 3801L → P in BAG52104. (PubMed:16303743)Curated
    Isoform 2 (identifier: Q9UJP4-2)
    Sequence conflicti534 – 5341G → D in BAA32314. (PubMed:9455484)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei502 – 53938HVGGS…PETRA → NFQAGQHWKHRLVLILQPKC HRDECLGSTAMMGGSHLN in isoform 2. 1 PublicationVSP_032563Add
    BLAST
    Alternative sequencei540 – 59758Missing in isoform 2. 1 PublicationVSP_032564Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007938 mRNA. Translation: BAA32314.2. Different initiation.
    AK075305 mRNA. Translation: BAG52104.1.
    AL591866 Genomic DNA. Translation: CAI16080.1.
    AL591866 Genomic DNA. Translation: CAI16082.1.
    CH471130 Genomic DNA. Translation: EAW71559.1.
    BC034039 mRNA. Translation: AAH34039.3.
    BC091648 mRNA. Translation: AAH91648.1.
    AK090472 mRNA. Translation: BAC03453.1.
    CCDSiCCDS30575.1. [Q9UJP4-1]
    RefSeqiNP_055666.2. NM_014851.2. [Q9UJP4-1]
    UniGeneiHs.7764.

    Genome annotation databases

    EnsembliENST00000377658; ENSP00000366886; ENSG00000162413. [Q9UJP4-1]
    ENST00000377663; ENSP00000366891; ENSG00000162413. [Q9UJP4-2]
    GeneIDi9903.
    KEGGihsa:9903.
    UCSCiuc001anz.1. human. [Q9UJP4-2]
    uc001aoa.3. human. [Q9UJP4-1]

    Polymorphism databases

    DMDMi172044863.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007938 mRNA. Translation: BAA32314.2 . Different initiation.
    AK075305 mRNA. Translation: BAG52104.1 .
    AL591866 Genomic DNA. Translation: CAI16080.1 .
    AL591866 Genomic DNA. Translation: CAI16082.1 .
    CH471130 Genomic DNA. Translation: EAW71559.1 .
    BC034039 mRNA. Translation: AAH34039.3 .
    BC091648 mRNA. Translation: AAH91648.1 .
    AK090472 mRNA. Translation: BAC03453.1 .
    CCDSi CCDS30575.1. [Q9UJP4-1 ]
    RefSeqi NP_055666.2. NM_014851.2. [Q9UJP4-1 ]
    UniGenei Hs.7764.

    3D structure databases

    ProteinModelPortali Q9UJP4.
    SMRi Q9UJP4. Positions 12-570.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115232. 8 interactions.
    STRINGi 9606.ENSP00000366886.

    PTM databases

    PhosphoSitei Q9UJP4.

    Polymorphism databases

    DMDMi 172044863.

    Proteomic databases

    MaxQBi Q9UJP4.
    PaxDbi Q9UJP4.
    PRIDEi Q9UJP4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377658 ; ENSP00000366886 ; ENSG00000162413 . [Q9UJP4-1 ]
    ENST00000377663 ; ENSP00000366891 ; ENSG00000162413 . [Q9UJP4-2 ]
    GeneIDi 9903.
    KEGGi hsa:9903.
    UCSCi uc001anz.1. human. [Q9UJP4-2 ]
    uc001aoa.3. human. [Q9UJP4-1 ]

    Organism-specific databases

    CTDi 9903.
    GeneCardsi GC01M006586.
    HGNCi HGNC:29041. KLHL21.
    HPAi HPA051364.
    neXtProti NX_Q9UJP4.
    PharmGKBi PA134989246.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264826.
    HOGENOMi HOG000261671.
    HOVERGENi HBG101644.
    InParanoidi Q9UJP4.
    KOi K10458.
    OMAi WVRADPP.
    OrthoDBi EOG7WHH8X.
    PhylomeDBi Q9UJP4.
    TreeFami TF329218.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi KLHL21. human.
    GenomeRNAii 9903.
    NextBioi 37341.
    PROi Q9UJP4.

    Gene expression databases

    ArrayExpressi Q9UJP4.
    Bgeei Q9UJP4.
    CleanExi HS_KLHL21.
    Genevestigatori Q9UJP4.

    Family and domain databases

    Gene3Di 2.130.10.80. 1 hit.
    3.30.710.10. 1 hit.
    InterProi IPR011705. BACK.
    IPR000210. BTB/POZ-like.
    IPR011333. BTB/POZ_fold.
    IPR013069. BTB_POZ.
    IPR015916. Gal_Oxidase_b-propeller.
    IPR017096. Kelch-like_gigaxonin-typ.
    IPR006652. Kelch_1.
    [Graphical view ]
    Pfami PF07707. BACK. 1 hit.
    PF00651. BTB. 1 hit.
    PF01344. Kelch_1. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
    SMARTi SM00875. BACK. 1 hit.
    SM00225. BTB. 1 hit.
    SM00612. Kelch. 5 hits.
    [Graphical view ]
    SUPFAMi SSF54695. SSF54695. 1 hit.
    PROSITEi PS50097. BTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
      Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
      DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Hippocampus and Lung carcinoma.
    6. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
      Jikuya H., Takano J., Kikuno R., Nagase T., Ohara O.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-597 (ISOFORM 1).
      Tissue: Spleen.
    7. Bienvenut W.V., Dhillon A.S., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 52-62; 99-122 AND 424-433 (ISOFORMS 1/2), PROTEIN SEQUENCE OF 561-571 (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    8. "Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases."
      Furukawa M., He Y.J., Borchers C., Xiong Y.
      Nat. Cell Biol. 5:1001-1007(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, INTERACTION WITH CUL3.
    9. "The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis."
      Maerki S., Olma M.H., Staubli T., Steigemann P., Gerlich D.W., Quadroni M., Sumara I., Peter M.
      J. Cell Biol. 187:791-800(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, MUTAGENESIS OF 114-ASP--GLN-117.

    Entry informationi

    Entry nameiKLH21_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJP4
    Secondary accession number(s): B3KQP2
    , O75057, Q5SY26, Q5SY28, Q8N4I6, Q8NF10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 114 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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

    External Data

    Dasty 3