Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y2M5 (KLH20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kelch-like protein 20
Alternative name(s):
Kelch-like ECT2-interacting protein
Kelch-like protein X
Gene names
Name:KLHL20
Synonyms:KLEIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length609 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 involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis (Ref.8). The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination (Ref.11). Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking (Ref.11). Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (Ref.10). In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression (Ref.9). Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of the BCR(KLHL20) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL20 and RBX1. Interacts with PDZ-RhoGEF/ARHGEF11, DAPK1, PML and CORO7. Interacts with F-actin. Interacts with IFN-gamma (IFNG). Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasmperinuclear region. Nucleus. Golgi apparatustrans-Golgi network. Cell projectionaxon By similarity. Cell projectiondendrite By similarity. Note: Localizes in the perinuclear region in normal conditions. Following IFN-alpha or IFN-gamma treatment, it is relocalized and sequestrated to the PML nuclear bodies, preventing DAPK1 ubiquitination (Ref.8). Ref.8 Ref.11

Induction

By hypoxia. Ref.9

Sequence similarities

Contains 1 BACK (BTB/Kelch associated) domain.

Contains 1 BTB (POZ) domain.

Contains 6 Kelch repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 609609Kelch-like protein 20
PRO_0000119123

Regions

Domain68 – 13568BTB
Domain170 – 272103BACK
Repeat319 – 36547Kelch 1
Repeat367 – 41347Kelch 2
Repeat414 – 46047Kelch 3
Repeat462 – 50746Kelch 4
Repeat509 – 55446Kelch 5
Repeat556 – 60146Kelch 6

Experimental info

Mutagenesis1091V → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-111; A-113; A-146; A-148 and A-150. Ref.8 Ref.9 Ref.10 Ref.11
Mutagenesis1111I → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-113; A-146; A-148 and A-150. Ref.8 Ref.9 Ref.10 Ref.11
Mutagenesis1131D → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-146; A-148 and A-150. Ref.8 Ref.9 Ref.10 Ref.11
Mutagenesis1461C → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-148 and A-150. Ref.8 Ref.9 Ref.10 Ref.11
Mutagenesis1481L → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-146 and A-150. Ref.8 Ref.9 Ref.10 Ref.11
Mutagenesis1501L → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-146 and A-148. Ref.8 Ref.9 Ref.10 Ref.11
Sequence conflict1711L → Q in BAG50912. Ref.3
Sequence conflict3211F → S in BAG50912. Ref.3
Sequence conflict3341S → N in BAG50912. Ref.3
Sequence conflict3961V → M in BAG50912. Ref.3
Sequence conflict5931G → W in BAA77027. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Y2M5 [UniParc].

Last modified September 1, 2009. Version 4.
Checksum: FA05E3FE8341B422

FASTA60967,955
        10         20         30         40         50         60 
MEGKPMRRCT NIRPGETGMD VTSRCTLGDP NKLPEGVPQP ARMPYISDKH PRQTLEVINL 

        70         80         90        100        110        120 
LRKHRELCDV VLVVGAKKIY AHRVILSACS PYFRAMFTGE LAESRQTEVV IRDIDERAME 

       130        140        150        160        170        180 
LLIDFAYTSQ ITVEEGNVQT LLPAACLLQL AEIQEACCEF LKRQLDPSNC LGIRAFADTH 

       190        200        210        220        230        240 
SCRELLRIAD KFTQHNFQEV MESEEFMLLP ANQLIDIISS DELNVRSEEQ VFNAVMAWVK 

       250        260        270        280        290        300 
YSIQERRPQL PQVLQHVRLP LLSPKFLVGT VGSDPLIKSD EECRDLVDEA KNYLLLPQER 

       310        320        330        340        350        360 
PLMQGPRTRP RKPIRCGEVL FAVGGWCSGD AISSVERYDP QTNEWRMVAS MSKRRCGVGV 

       370        380        390        400        410        420 
SVLDDLLYAV GGHDGSSYLN SVERYDPKTN QWSSDVAPTS TCRTSVGVAV LGGFLYAVGG 

       430        440        450        460        470        480 
QDGVSCLNIV ERYDPKENKW TRVASMSTRR LGVAVAVLGG FLYAVGGSDG TSPLNTVERY 

       490        500        510        520        530        540 
NPQENRWHTI APMGTRRKHL GCAVYQDMIY AVGGRDDTTE LSSAERYNPR TNQWSPVVAM 

       550        560        570        580        590        600 
TSRRSGVGLA VVNGQLMAVG GFDGTTYLKT IEVFDPDANT WRLYGGMNYR RLGGGVGVIK 


MTHCESHIW 

« Hide

References

« Hide 'large scale' references
[1]"Novel kelch-like protein, KLEIP, is involved in actin assembly at cell-cell contact sites of Madin-Darby canine kidney cells."
Hara T., Ishida H., Raziuddin R., Dorkhom S., Kamijo K., Miki T.
Mol. Biol. Cell 15:1172-1184(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ACTIN.
[2]"Kelch motif containing protein."
Yoshida K., Sugano S.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[4]"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].
[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].
[6]"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.
[7]"The BTB-Kelch protein KLEIP controls endothelial migration and sprouting angiogenesis."
Nacak T.G., Alajati A., Leptien K., Fulda C., Weber H., Miki T., Czepluch F.S., Waltenberger J., Wieland T., Augustin H.G., Kroll J.
Circ. Res. 100:1155-1163(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responses."
Lee Y.R., Yuan W.C., Ho H.C., Chen C.H., Shih H.M., Chen R.H.
EMBO J. 29:1748-1761(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INTERACTION WITH DAPK AND IFNG, MUTAGENESIS OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
[9]"A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to potentiate HIF-1 signaling and prostate cancer progression."
Yuan W.C., Lee Y.R., Huang S.F., Lin Y.M., Chen T.Y., Chung H.C., Tsai C.H., Chen H.Y., Chiang C.T., Lai C.K., Lu L.T., Chen C.H., Gu D.L., Pu Y.S., Jou Y.S., Lu K.P., Hsiao P.W., Shih H.M., Chen R.H.
Cancer Cell 20:214-228(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PML, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INDUCTION, MUTAGENESIS OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
[10]"PDZ-RhoGEF ubiquitination by Cullin3-KLHL20 controls neurotrophin-induced neurite outgrowth."
Lin M.Y., Lin Y.M., Kao T.C., Chuang H.H., Chen R.H.
J. Cell Biol. 193:985-994(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARHGEF11, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, MUTAGENESIS OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
[11]"K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3 ligase regulates protein trafficking."
Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C., Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.
Mol. Cell 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INTERACTION WITH CORO7, MUTAGENESIS OF VAL-109; ILE-111; ASP-113; CYS-146; LEU-148 AND LEU-150.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ844466 mRNA. Translation: CAH59617.1.
AB026190 mRNA. Translation: BAA77027.1.
AK001430 mRNA. Translation: BAG50912.1.
AL109921, BX248409 Genomic DNA. Translation: CAI20377.1.
BX248409, AL109921 Genomic DNA. Translation: CAH73000.1.
BC063418 mRNA. Translation: AAH63418.1.
CCDSCCDS1310.1.
RefSeqNP_055273.2. NM_014458.3.
XP_005245150.1. XM_005245093.1.
UniGeneHs.495035.

3D structure databases

ProteinModelPortalQ9Y2M5.
SMRQ9Y2M5. Positions 50-599.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118100. 18 interactions.
IntActQ9Y2M5. 16 interactions.
MINTMINT-6783961.
STRING9606.ENSP00000209884.

PTM databases

PhosphoSiteQ9Y2M5.

Polymorphism databases

DMDM257051084.

Proteomic databases

MaxQBQ9Y2M5.
PaxDbQ9Y2M5.
PRIDEQ9Y2M5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000209884; ENSP00000209884; ENSG00000076321.
GeneID27252.
KEGGhsa:27252.
UCSCuc001gjc.3. human.

Organism-specific databases

CTD27252.
GeneCardsGC01P173684.
HGNCHGNC:25056. KLHL20.
HPAHPA025034.
neXtProtNX_Q9Y2M5.
PharmGKBPA134982126.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236397.
HOGENOMHOG000230814.
HOVERGENHBG014286.
InParanoidQ9Y2M5.
KOK10457.
OMAPMSKRRC.
OrthoDBEOG7ZWD17.
PhylomeDBQ9Y2M5.
TreeFamTF329218.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9Y2M5.
BgeeQ9Y2M5.
CleanExHS_KLHL20.
GenevestigatorQ9Y2M5.

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. 6 hits.
[Graphical view]
PIRSFPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
PROSITEPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKLHL20.
GenomeRNAi27252.
NextBio50186.
PROQ9Y2M5.

Entry information

Entry nameKLH20_HUMAN
AccessionPrimary (citable) accession number: Q9Y2M5
Secondary accession number(s): B3KMA0 expand/collapse secondary AC list , Q5TZF2, Q5ZF45, Q9H457
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 115 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