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Q9UJP4

- KLH21_HUMAN

UniProt

Q9UJP4 - KLH21_HUMAN

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Protein
Kelch-like protein 21
Gene
KLHL21, KIAA0469
Organism
Homo sapiens (Human)
Status
Reviewed - 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 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
Complete GO annotation...

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

GO - Cellular componenti

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

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 21
PRO_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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 BTB (POZ) domain.
Contains 6 Kelch repeats.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei502 – 53938HVGGS…PETRA → NFQAGQHWKHRLVLILQPKC HRDECLGSTAMMGGSHLN in isoform 2.
VSP_032563Add
BLAST
Alternative sequencei540 – 59758Missing in isoform 2.
VSP_032564Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 113 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

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