SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y2M5

- KLH20_HUMAN

UniProt

Q9Y2M5 - KLH20_HUMAN

(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)

Protein

Kelch-like protein 20

Gene
KLHL20, KLEIP
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 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 (1 Publication). The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination (1 Publication). 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 (1 Publication). 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 (1 Publication). 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 (1 Publication).6 Publications

Pathwayi

GO - Molecular functioni

  1. interferon-gamma binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cytoskeleton organization Source: ProtInc
  2. negative regulation of apoptotic process Source: UniProtKB
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. protein ubiquitination Source: UniProtKB
  5. response to interferon-alpha Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport, Ubl conjugation pathway

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Kelch-like protein 20
Alternative name(s):
Kelch-like ECT2-interacting protein
Kelch-like protein X
Gene namesi
Name:KLHL20
Synonyms:KLEIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:25056. KLHL20.

Subcellular locationi

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 (1 Publication).2 Publications

GO - Cellular componenti

  1. actin cytoskeleton Source: ProtInc
  2. Cul3-RING ubiquitin ligase complex Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. Golgi apparatus Source: HPA
  5. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  6. PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Golgi apparatus, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091V → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-111; A-113; A-146; A-148 and A-150. 4 Publications
Mutagenesisi111 – 1111I → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-113; A-146; A-148 and A-150. 4 Publications
Mutagenesisi113 – 1131D → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-146; A-148 and A-150. 4 Publications
Mutagenesisi146 – 1461C → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-148 and A-150. 4 Publications
Mutagenesisi148 – 1481L → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-146 and A-150. 4 Publications
Mutagenesisi150 – 1501L → A in KLHL20m6; abolishes interaction with CUL3; when associated with A-109; A-111; A-113; A-146 and A-148. 4 Publications

Organism-specific databases

PharmGKBiPA134982126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 609609Kelch-like protein 20PRO_0000119123Add
BLAST

Proteomic databases

MaxQBiQ9Y2M5.
PaxDbiQ9Y2M5.
PRIDEiQ9Y2M5.

PTM databases

PhosphoSiteiQ9Y2M5.

Expressioni

Inductioni

By hypoxia.1 Publication

Gene expression databases

ArrayExpressiQ9Y2M5.
BgeeiQ9Y2M5.
CleanExiHS_KLHL20.
GenevestigatoriQ9Y2M5.

Organism-specific databases

HPAiHPA025034.

Interactioni

Subunit structurei

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).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL3Q136182EBI-714379,EBI-456129
DAPK1P5335511EBI-714379,EBI-358616
PMLP295909EBI-714379,EBI-295890
PRMT6Q96LA82EBI-714379,EBI-912440

Protein-protein interaction databases

BioGridi118100. 19 interactions.
IntActiQ9Y2M5. 16 interactions.
MINTiMINT-6783961.
STRINGi9606.ENSP00000209884.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2M5.
SMRiQ9Y2M5. Positions 50-599.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 13568BTBAdd
BLAST
Domaini170 – 272103BACKAdd
BLAST
Repeati319 – 36547Kelch 1Add
BLAST
Repeati367 – 41347Kelch 2Add
BLAST
Repeati414 – 46047Kelch 3Add
BLAST
Repeati462 – 50746Kelch 4Add
BLAST
Repeati509 – 55446Kelch 5Add
BLAST
Repeati556 – 60146Kelch 6Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiNOG236397.
HOGENOMiHOG000230814.
HOVERGENiHBG014286.
InParanoidiQ9Y2M5.
KOiK10457.
OMAiPMSKRRC.
OrthoDBiEOG7ZWD17.
PhylomeDBiQ9Y2M5.
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. 6 hits.
[Graphical view]
PIRSFiPIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTiSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y2M5-1 [UniParc]FASTAAdd to Basket

« Hide

MEGKPMRRCT NIRPGETGMD VTSRCTLGDP NKLPEGVPQP ARMPYISDKH    50
PRQTLEVINL LRKHRELCDV VLVVGAKKIY AHRVILSACS PYFRAMFTGE 100
LAESRQTEVV IRDIDERAME LLIDFAYTSQ ITVEEGNVQT LLPAACLLQL 150
AEIQEACCEF LKRQLDPSNC LGIRAFADTH SCRELLRIAD KFTQHNFQEV 200
MESEEFMLLP ANQLIDIISS DELNVRSEEQ VFNAVMAWVK YSIQERRPQL 250
PQVLQHVRLP LLSPKFLVGT VGSDPLIKSD EECRDLVDEA KNYLLLPQER 300
PLMQGPRTRP RKPIRCGEVL FAVGGWCSGD AISSVERYDP QTNEWRMVAS 350
MSKRRCGVGV SVLDDLLYAV GGHDGSSYLN SVERYDPKTN QWSSDVAPTS 400
TCRTSVGVAV LGGFLYAVGG QDGVSCLNIV ERYDPKENKW TRVASMSTRR 450
LGVAVAVLGG FLYAVGGSDG TSPLNTVERY NPQENRWHTI APMGTRRKHL 500
GCAVYQDMIY AVGGRDDTTE LSSAERYNPR TNQWSPVVAM TSRRSGVGLA 550
VVNGQLMAVG GFDGTTYLKT IEVFDPDANT WRLYGGMNYR RLGGGVGVIK 600
MTHCESHIW 609
Length:609
Mass (Da):67,955
Last modified:September 1, 2009 - v4
Checksum:iFA05E3FE8341B422
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711L → Q in BAG50912. 1 Publication
Sequence conflicti321 – 3211F → S in BAG50912. 1 Publication
Sequence conflicti334 – 3341S → N in BAG50912. 1 Publication
Sequence conflicti396 – 3961V → M in BAG50912. 1 Publication
Sequence conflicti593 – 5931G → W in BAA77027. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1310.1.
RefSeqiNP_055273.2. NM_014458.3.
XP_005245150.1. XM_005245093.1.
UniGeneiHs.495035.

Genome annotation databases

EnsembliENST00000209884; ENSP00000209884; ENSG00000076321.
GeneIDi27252.
KEGGihsa:27252.
UCSCiuc001gjc.3. human.

Polymorphism databases

DMDMi257051084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1310.1.
RefSeqi NP_055273.2. NM_014458.3.
XP_005245150.1. XM_005245093.1.
UniGenei Hs.495035.

3D structure databases

ProteinModelPortali Q9Y2M5.
SMRi Q9Y2M5. Positions 50-599.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118100. 19 interactions.
IntActi Q9Y2M5. 16 interactions.
MINTi MINT-6783961.
STRINGi 9606.ENSP00000209884.

PTM databases

PhosphoSitei Q9Y2M5.

Polymorphism databases

DMDMi 257051084.

Proteomic databases

MaxQBi Q9Y2M5.
PaxDbi Q9Y2M5.
PRIDEi Q9Y2M5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000209884 ; ENSP00000209884 ; ENSG00000076321 .
GeneIDi 27252.
KEGGi hsa:27252.
UCSCi uc001gjc.3. human.

Organism-specific databases

CTDi 27252.
GeneCardsi GC01P173684.
HGNCi HGNC:25056. KLHL20.
HPAi HPA025034.
neXtProti NX_Q9Y2M5.
PharmGKBi PA134982126.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236397.
HOGENOMi HOG000230814.
HOVERGENi HBG014286.
InParanoidi Q9Y2M5.
KOi K10457.
OMAi PMSKRRC.
OrthoDBi EOG7ZWD17.
PhylomeDBi Q9Y2M5.
TreeFami TF329218.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikii KLHL20.
GenomeRNAii 27252.
NextBioi 50186.
PROi Q9Y2M5.

Gene expression databases

ArrayExpressi Q9Y2M5.
Bgeei Q9Y2M5.
CleanExi HS_KLHL20.
Genevestigatori Q9Y2M5.

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. 6 hits.
[Graphical view ]
PIRSFi PIRSF037037. Kelch-like_protein_gigaxonin. 1 hit.
SMARTi SM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
PROSITEi PS50097. BTB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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 54:586-600(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.

Entry informationi

Entry nameiKLH20_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2M5
Secondary accession number(s): B3KMA0
, Q5TZF2, Q5ZF45, Q9H457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: September 1, 2009
Last modified: September 3, 2014
This is version 116 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, 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

Similar proteinsi