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Q9UH77 (KLHL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 3
Gene names
Name:KLHL3
Synonyms:KIAA1129
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of ion transport in the distal nephron. The BCR(KLHL3) complex acts by mediating ubiquitination of WNK4, an inhibitor of potassium channel KCNJ1, leading to WNK4 degradation. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of the BCR(KLHL3) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL3 and RBX1 Probable. Interacts with SLC12A3. Interacts with WNK1 and WNK4. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcytosol Ref.13.

Tissue specificity

Widely expressed. Ref.13

Involvement in disease

Pseudohypoaldosteronism 2D (PHA2D) [MIM:614495]: A disorder characterized by severe hypertension, hyperkalemia, hyperchloremia, hyperchloremic metabolic acidosis, and correction of physiologic abnormalities by thiazide diuretics. PHA2D inheritance is autosomal dominant or recessive.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13

Sequence similarities

Contains 1 BACK (BTB/Kelch associated) domain.

Contains 1 BTB (POZ) domain.

Contains 6 Kelch repeats.

Caution

The BCR(KLHL3) complex was initially thought to act by mediating ubiquitination of SLC12A3/NCC (Ref.13). However, it was later shown that effects on SLC12A3/NCC are indirect and caused by impaired ubiquitination of WNK4 (Ref.7).

Sequence caution

The sequence AAB97127.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAA86443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9UH77-1)

Also known as: KLHL3A;

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 B (identifier: Q9UH77-2)

Also known as: KLHL3B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
Isoform C (identifier: Q9UH77-3)

Also known as: KLHL3C;

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Kelch-like protein 3
PRO_0000119103

Regions

Domain50 – 11768BTB
Domain152 – 254103BACK
Repeat302 – 34746Kelch 1
Repeat348 – 39447Kelch 2
Repeat396 – 44146Kelch 3
Repeat442 – 49049Kelch 4
Repeat491 – 53747Kelch 5
Repeat539 – 58547Kelch 6

Natural variations

Alternative sequence1 – 8282Missing in isoform C.
VSP_002817
Alternative sequence1 – 3232Missing in isoform B.
VSP_002816
Natural variant771A → E in PHA2D; impaired interaction with CUL3. Ref.7 Ref.9 Ref.12
VAR_067501
Natural variant781M → V in PHA2D; impaired interaction with CUL3. Ref.7 Ref.12
Corresponds to variant rs199469624 [ dbSNP | Ensembl ].
VAR_067502
Natural variant851E → A in PHA2D; impaired interaction with CUL3. Ref.7 Ref.12
VAR_067503
Natural variant1641C → F in PHA2D; impaired interaction with CUL3; de novo mutation. Ref.7 Ref.9 Ref.12
VAR_067504
Natural variant2281R → G in PHA2D. Ref.13
VAR_067505
Natural variant3091Q → R in PHA2D; impaired interaction with WNK1. Ref.7 Ref.9 Ref.12
VAR_067506
Natural variant3221F → C in PHA2D. Ref.12
VAR_067507
Natural variant3361R → I in PHA2D. Ref.12
VAR_067508
Natural variant3401A → V in PHA2D; does not affect interaction with WNK1 or CUL3. Ref.7 Ref.12
VAR_067509
Natural variant3611V → M in PHA2D. Ref.13
VAR_067510
Natural variant3621R → W in PHA2D. Ref.13
Corresponds to variant rs200892557 [ dbSNP | Ensembl ].
VAR_067511
Natural variant3841R → Q in PHA2D. Ref.7 Ref.12
VAR_067512
Natural variant3841R → W in PHA2D; impaired interaction with WNK1. Ref.13
VAR_067513
Natural variant3871L → P in PHA2D; impaired interaction with WNK1. Ref.7 Ref.9 Ref.12
VAR_067514
Natural variant3981A → V in PHA2D. Ref.13
VAR_067515
Natural variant4101S → L in PHA2D; impaired interaction with WNK1. Ref.7 Ref.12 Ref.13
VAR_067516
Natural variant4261P → L in PHA2D. Ref.13
VAR_067517
Natural variant4271M → T in PHA2D. Ref.12
VAR_067518
Natural variant4311R → Q in PHA2D. Ref.12
VAR_067519
Natural variant4321S → N in PHA2D; impaired interaction with WNK1. Ref.7 Ref.12 Ref.13
VAR_067520
Natural variant4331S → G in PHA2D. Ref.13
VAR_067521
Natural variant4331S → N in PHA2D. Ref.7 Ref.12
VAR_067522
Natural variant4381V → I Found in a patient with hypertension; unknown pathological significance. Ref.12
VAR_067523
Natural variant4941A → T in PHA2D; does not affect interaction with WNK1 or CUL3. Ref.7 Ref.12
VAR_067524
Natural variant5001G → V in PHA2D. Ref.13
VAR_067525
Natural variant5011P → T in PHA2D. Ref.12
VAR_067526
Natural variant5281R → C in PHA2D; impaired interaction with WNK1. Ref.7 Ref.9 Ref.12 Ref.13
VAR_067527
Natural variant5281R → H in PHA2D; impaired interaction with WNK1 and WNK4 and impaired ubiquitination of WNK4. Ref.7 Ref.8 Ref.10 Ref.12 Ref.13
VAR_067528
Natural variant5291N → K in PHA2D; impaired interaction with WNK1. Ref.7 Ref.13
VAR_067529
Natural variant5571Y → C in PHA2D. Ref.12
VAR_067530
Natural variant5751R → W in PHA2D. Ref.12
VAR_067531

Experimental info

Sequence conflict2271T → N in AAF20938. Ref.1

Secondary structure

............................................................. 587
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (KLHL3A) [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: C5026A246620BEA1

FASTA58764,970
        10         20         30         40         50         60 
MEGESVKLSS QTLIQAGDDE KNQRTITVNP AHMGKAFKVM NELRSKQLLC DVMIVAEDVE 

        70         80         90        100        110        120 
IEAHRVVLAA CSPYFCAMFT GDMSESKAKK IEIKDVDGQT LSKLIDYIYT AEIEVTEENV 

       130        140        150        160        170        180 
QVLLPAASLL QLMDVRQNCC DFLQSQLHPT NCLGIRAFAD VHTCTDLLQQ ANAYAEQHFP 

       190        200        210        220        230        240 
EVMLGEEFLS LSLDQVCSLI SSDKLTVSSE EKVFEAVISW INYEKETRLE HMAKLMEHVR 

       250        260        270        280        290        300 
LPLLPRDYLV QTVEEEALIK NNNTCKDFLI EAMKYHLLPL DQRLLIKNPR TKPRTPVSLP 

       310        320        330        340        350        360 
KVMIVVGGQA PKAIRSVECY DFEEDRWDQI AELPSRRCRA GVVFMAGHVY AVGGFNGSLR 

       370        380        390        400        410        420 
VRTVDVYDGV KDQWTSIASM QERRSTLGAA VLNDLLYAVG GFDGSTGLAS VEAYSYKTNE 

       430        440        450        460        470        480 
WFFVAPMNTR RSSVGVGVVE GKLYAVGGYD GASRQCLSTV EQYNPATNEW IYVADMSTRR 

       490        500        510        520        530        540 
SGAGVGVLSG QLYATGGHDG PLVRKSVEVY DPGTNTWKQV ADMNMCRRNA GVCAVNGLLY 

       550        560        570        580 
VVGGDDGSCN LASVEYYNPV TDKWTLLPTN MSTGRSYAGV AVIHKSL 

« Hide

Isoform B (KLHL3B) [UniParc].

Checksum: 1FE9B061BD542347
Show »

FASTA55561,490
Isoform C (KLHL3C) [UniParc].

Checksum: 0B4157AC6E474F70
Show »

FASTA50555,927

References

« Hide 'large scale' references
[1]"Molecular characterization of KLHL3, a human homologue of the Drosophila kelch gene."
Lai F., Orelli B.J., Till B.G., Godley L.A., Fernald A.A., Pamintuan L., Le Beau M.M.
Genomics 66:65-75(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), ALTERNATIVE SPLICING.
Tissue: Bone marrow.
[2]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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] (ISOFORM A).
Tissue: Kidney.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 CUL3-KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in KLHL3 and WNK4 disrupt interaction."
Ohta A., Schumacher F.R., Mehellou Y., Johnson C., Knebel A., Macartney T.J., Wood N.T., Alessi D.R., Kurz T.
Biochem. J. 451:111-122(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CUL3; WNK1 AND WNK4, CHARACTERIZATION OF VARIANTS VARIANTS PHA2D GLU-77; VAL-78; ALA-85; PHE-164; ARG-309; VAL-340; GLN-384; PRO-387; LEU-410; ASN-432; ASN-433; THR-494; HIS-528; CYS-528 AND LYS-529.
[8]"Impaired KLHL3-mediated ubiquitination of WNK4 causes human hypertension."
Wakabayashi M., Mori T., Isobe K., Sohara E., Susa K., Araki Y., Chiga M., Kikuchi E., Nomura N., Mori Y., Matsuo H., Murata T., Nomura S., Asano T., Kawaguchi H., Nonoyama S., Rai T., Sasaki S., Uchida S.
Cell Rep. 3:858-868(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INTERACTION WITH WNK4 AND CUL3, CHARACTERIZATION OF VARIANT PHA2D HIS-528.
[9]"Disease-causing mutations in KLHL3 impair its effect on WNK4 degradation."
Wu G., Peng J.B.
FEBS Lett. 587:1717-1722(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH WNK4, CHARACTERIZATION OF VARIANTS VARIANTS PHA2D GLU-77; PHE-164; ARG-309; PRO-387 AND CYS-528.
[10]"Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via ubiquitination and degradation of WNK4."
Shibata S., Zhang J., Puthumana J., Stone K.L., Lifton R.P.
Proc. Natl. Acad. Sci. U.S.A. 110:7838-7843(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INTERACTION WITH WNK1; WNK4 AND CUL3, CHARACTERIZATION OF VARIANT PHA2D HIS-528.
[11]"Crystal structure of KLHL3 in complex with Cullin3."
Ji A.X., Prive G.G.
PLoS ONE 8:E60445-E60445(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) OF 24-276 IN COMPLEX WITH CUL3.
[12]"Mutations in kelch-like 3 and cullin 3 cause hypertension and electrolyte abnormalities."
Boyden L.M., Choi M., Choate K.A., Nelson-Williams C.J., Farhi A., Toka H.R., Tikhonova I.R., Bjornson R., Mane S.M., Colussi G., Lebel M., Gordon R.D., Semmekrot B.A., Poujol A., Valimaki M.J., De Ferrari M.E., Sanjad S.A., Gutkin M. expand/collapse author list , Karet F.E., Tucci J.R., Stockigt J.R., Keppler-Noreuil K.M., Porter C.C., Anand S.K., Whiteford M.L., Davis I.D., Dewar S.B., Bettinelli A., Fadrowski J.J., Belsha C.W., Hunley T.E., Nelson R.D., Trachtman H., Cole T.R., Pinsk M., Bockenhauer D., Shenoy M., Vaidyanathan P., Foreman J.W., Rasoulpour M., Thameem F., Al-Shahrouri H.Z., Radhakrishnan J., Gharavi A.G., Goilav B., Lifton R.P.
Nature 482:98-102(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PHA2D GLU-77; VAL-78; ALA-85; PHE-164; ARG-309; CYS-322; ILE-336; VAL-340; GLN-384; PRO-387; LEU-410; THR-427; GLN-431; ASN-432; ASN-433; THR-494; THR-501; HIS-528; CYS-528; CYS-557 AND TRP-575, VARIANT ILE-438.
[13]"KLHL3 mutations cause familial hyperkalemic hypertension by impairing ion transport in the distal nephron."
Louis-Dit-Picard H., Barc J., Trujillano D., Miserey-Lenkei S., Bouatia-Naji N., Pylypenko O., Beaurain G., Bonnefond A., Sand O., Simian C., Vidal-Petiot E., Soukaseum C., Mandet C., Broux F., Chabre O., Delahousse M., Esnault V., Fiquet B. expand/collapse author list , Houillier P., Bagnis C.I., Koenig J., Konrad M., Landais P., Mourani C., Niaudet P., Probst V., Thauvin C., Unwin R.J., Soroka S.D., Ehret G., Ossowski S., Caulfield M., Bruneval P., Estivill X., Froguel P., Hadchouel J., Schott J.J., Jeunemaitre X.
Nat. Genet. 44:456-460(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PHA2D GLY-228; MET-361; TRP-362; TRP-384; VAL-398; LEU-410; LEU-426; ASN-432; GLY-433; VAL-500; HIS-528; CYS-528 AND LYS-529, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SLC12A3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF208068 mRNA. Translation: AAF20938.1.
AF208069 mRNA. Translation: AAF20939.1.
AF208070 mRNA. Translation: AAF20995.1.
AB032955 mRNA. Translation: BAA86443.1. Different initiation.
AK314707 mRNA. Translation: BAG37254.1.
AC004021 Genomic DNA. Translation: AAB97127.1. Sequence problems.
AC092318 Genomic DNA. No translation available.
AC106775 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW62183.1.
CCDSCCDS4192.1. [Q9UH77-1]
CCDS58969.1. [Q9UH77-3]
CCDS58970.1. [Q9UH77-2]
RefSeqNP_001244123.1. NM_001257194.1. [Q9UH77-2]
NP_001244124.1. NM_001257195.1. [Q9UH77-3]
NP_059111.2. NM_017415.2. [Q9UH77-1]
UniGeneHs.655084.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4CH9X-ray1.84A/B298-587[»]
4HXIX-ray3.51A24-276[»]
ProteinModelPortalQ9UH77.
SMRQ9UH77. Positions 29-260, 300-585.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117637. 9 interactions.
IntActQ9UH77. 2 interactions.
STRING9606.ENSP00000312397.

PTM databases

PhosphoSiteQ9UH77.

Polymorphism databases

DMDM13431657.

Proteomic databases

PaxDbQ9UH77.
PRIDEQ9UH77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309755; ENSP00000312397; ENSG00000146021. [Q9UH77-1]
ENST00000506491; ENSP00000424828; ENSG00000146021. [Q9UH77-3]
ENST00000508657; ENSP00000422099; ENSG00000146021. [Q9UH77-2]
GeneID26249.
KEGGhsa:26249.
UCSCuc003lbr.5. human. [Q9UH77-1]

Organism-specific databases

CTD26249.
GeneCardsGC05M136953.
HGNCHGNC:6354. KLHL3.
HPAHPA051291.
MIM605775. gene.
614495. phenotype.
neXtProtNX_Q9UH77.
Orphanet300525. Pseudohypoaldosteronism type 2D.
PharmGKBPA30144.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149197.
HOGENOMHOG000230814.
HOVERGENHBG014286.
KOK10443.
OMARSKRLLC.
OrthoDBEOG7ZWD17.
PhylomeDBQ9UH77.
TreeFamTF329218.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9UH77.
BgeeQ9UH77.
CleanExHS_KLHL3.
GenevestigatorQ9UH77.

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

ChiTaRSKLHL3. human.
GeneWikiKLHL3.
GenomeRNAi26249.
NextBio48460.
PROQ9UH77.
SOURCESearch...

Entry information

Entry nameKLHL3_HUMAN
AccessionPrimary (citable) accession number: Q9UH77
Secondary accession number(s): B2RBK7 expand/collapse secondary AC list , Q9UH75, Q9UH76, Q9ULU0, Q9Y6V6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 119 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM