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Q9UJP4 (KLH21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kelch-like protein 21
Gene names
Name:KLHL21
Synonyms:KIAA0469
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length597 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of the BCR(KLHL21) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL21 and RBX1. Ref.9

Subcellular location

Cytoplasmcytoskeletonspindle. Note: Localizes to the spindle midzone and targets CUL3 to this region. Ref.9

Sequence similarities

Contains 1 BACK (BTB/Kelch associated) domain.

Contains 1 BTB (POZ) domain.

Contains 6 Kelch repeats.

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJP4-1)

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.
Isoform 2 (identifier: Q9UJP4-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 597597Kelch-like protein 21
PRO_0000119125

Regions

Domain35 – 10369BTB
Domain138 – 239102BACK
Repeat287 – 33549Kelch 1
Repeat336 – 38247Kelch 2
Repeat384 – 42239Kelch 3
Repeat423 – 47048Kelch 4
Repeat472 – 51241Kelch 5
Repeat513 – 56048Kelch 6

Natural variations

Alternative sequence502 – 53938HVGGS…PETRA → NFQAGQHWKHRLVLILQPKC HRDECLGSTAMMGGSHLN in isoform 2.
VSP_032563
Alternative sequence540 – 59758Missing in isoform 2.
VSP_032564

Experimental info

Mutagenesis114 – 1174DLLQ → AALA: Abolishes interaction with CUL3. Ref.9
Sequence conflict1831R → C in BAC03453. Ref.6
Sequence conflict3801L → P in BAG52104. Ref.2
Isoform 2:
Sequence conflict5341G → D in BAA32314. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 18, 2008. Version 4.
Checksum: D3E682609F284645

FASTA59766,617
        10         20         30         40         50         60 
MERPAPLAVL PFSDPAHALS LLRGLSQLRA ERKFLDVTLE AAGGRDFPAH RAVLAAASPY 

        70         80         90        100        110        120 
FRAMFAGQLR ESRAERVRLH GVPPDMLQLL LDFSYTGRVA VSGDNAEPLL RAADLLQFPA 

       130        140        150        160        170        180 
VKEACGAFLQ QQLDLANCLD MQDFAEAFSC SGLASAAQRF ILRHVGELGA EQLERLPLAR 

       190        200        210        220        230        240 
LLRYLRDDGL CVPKEEAAYQ LALRWVRADP PRRAAHWPQL LEAVRLPFVR RFYLLAHVEA 

       250        260        270        280        290        300 
EPLVARCPPC LRLLREARDF QAARYDRHDR GPCPRMRPRP STGLAEILVL VGGCDQDCDE 

       310        320        330        340        350        360 
LVTVDCYNPQ TGQWRYLAEF PDHLGGGYSI VALGNDIYVT GGSDGSRLYD CVWRYNSSVN 

       370        380        390        400        410        420 
EWAEVAPMLK AREYHSSSVL DGLLYVVAAD STERYDHTTD SWEALQPMTY PMDNCSTTAC 

       430        440        450        460        470        480 
RGRLYAIGSL AGKETMVMQC YDPDTDLWSL VDCGQLPPWS FAPKTATLNG LMYFVRDDSA 

       490        500        510        520        530        540 
EVDVYNPTRN EWDKIPSMNQ VHVGGSLAVL GGKLYVSGGY DNTFELSDVV EAYDPETRAW 

       550        560        570        580        590 
SVVGRLPEPT FWHGSVSIFR QFMPQTFSGG RGFELDSGSD DMDPGRPRPP RDPDELH 

« Hide

Isoform 2 [UniParc].

Checksum: DDE88D184C05A945
Show »

FASTA53960,378

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055666.2. NM_014851.2.
UniGeneHs.7764.

3D structure databases

ProteinModelPortalQ9UJP4.
SMRQ9UJP4. Positions 12-570.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115232. 7 interactions.
STRING9606.ENSP00000366886.

PTM databases

PhosphoSiteQ9UJP4.

Polymorphism databases

DMDM172044863.

Proteomic databases

PaxDbQ9UJP4.
PRIDEQ9UJP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377658; ENSP00000366886; ENSG00000162413. [Q9UJP4-1]
ENST00000377663; ENSP00000366891; ENSG00000162413. [Q9UJP4-2]
GeneID9903.
KEGGhsa:9903.
UCSCuc001anz.1. human. [Q9UJP4-2]
uc001aoa.3. human. [Q9UJP4-1]

Organism-specific databases

CTD9903.
GeneCardsGC01M006586.
HGNCHGNC:29041. KLHL21.
HPAHPA051364.
neXtProtNX_Q9UJP4.
PharmGKBPA134989246.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264826.
HOGENOMHOG000261671.
HOVERGENHBG101644.
InParanoidQ9UJP4.
KOK10458.
OMAWVRADPP.
OrthoDBEOG7WHH8X.
PhylomeDBQ9UJP4.
TreeFamTF329218.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UJP4.
BgeeQ9UJP4.
CleanExHS_KLHL21.
GenevestigatorQ9UJP4.

Family and domain databases

Gene3D2.130.10.80. 1 hit.
3.30.710.10. 1 hit.
InterProIPR011705. 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]
PfamPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 3 hits.
[Graphical view]
PIRSFPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 5 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKLHL21. human.
GenomeRNAi9903.
NextBio37341.
PROQ9UJP4.

Entry information

Entry nameKLH21_HUMAN
AccessionPrimary (citable) accession number: Q9UJP4
Secondary accession number(s): B3KQP2 expand/collapse secondary AC list , O75057, Q5SY26, Q5SY28, Q8N4I6, Q8NF10
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 110 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM