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Q53G59

- KLH12_HUMAN

UniProt

Q53G59 - KLH12_HUMAN

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Protein

Kelch-like protein 12

Gene

KLHL12

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 ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport. The BCR(KLHL12) complex is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). As part of the BCR(KLHL12) complex, also acts as a negative regulator of the Wnt signaling pathway by mediating ubiquitination and subsequent proteolysis of DVL3. The BCR(KLHL12) complex also mediates polyubiquitination of DRD4, without leading to degradation of DRD4.4 Publications

Pathwayi

GO - Biological processi

  1. COPII vesicle coating Source: UniProtKB
  2. ER to Golgi vesicle-mediated transport Source: UniProtKB
  3. protein monoubiquitination Source: UniProtKB
  4. Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Transport, Ubl conjugation pathway, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_200841. degradation of DVL.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Kelch-like protein 12
Alternative name(s):
CUL3-interacting protein 1
DKIR homolog
Short name:
hDKIR
Gene namesi
Name:KLHL12
Synonyms:C3IP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:19360. KLHL12.

Subcellular locationi

Cytoplasmic vesicleCOPII-coated vesicle 1 Publication

GO - Cellular componenti

  1. Cul3-RING ubiquitin ligase complex Source: UniProtKB
  2. ER to Golgi transport vesicle Source: UniProtKB
  3. Golgi membrane Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi289 – 2902FG → AA: Abolishes interaction with SEC31A and subsequent monoubiquitination of SEC31A. 1 Publication

Organism-specific databases

PharmGKBiPA134952416.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 568568Kelch-like protein 12PRO_0000234349Add
BLAST

Proteomic databases

MaxQBiQ53G59.
PaxDbiQ53G59.
PRIDEiQ53G59.

PTM databases

PhosphoSiteiQ53G59.

Expressioni

Tissue specificityi

Ubiquitously expressed. Highly expressed in testis and at lower levels in the submandibular salivary gland.2 Publications

Gene expression databases

BgeeiQ53G59.
CleanExiHS_KLHL12.
ExpressionAtlasiQ53G59. baseline and differential.
GenevestigatoriQ53G59.

Interactioni

Subunit structurei

Component of the BCR(KLHL12) E3 ubiquitin ligase complex, at least composed of CUL3 and KLHL12 and RBX1. This complex interacts with DVL3 upon activation of the Wnt signaling pathway by WNT3A. Interacts with DRD4, KLHL12 and SEC31A.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN1P542532EBI-740929,EBI-930964
PEF1Q9UBV82EBI-740929,EBI-724639

Protein-protein interaction databases

BioGridi121890. 30 interactions.
IntActiQ53G59. 21 interactions.
MINTiMINT-1434520.
STRINGi9606.ENSP00000356230.

Structurei

Secondary structure

1
568
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi281 – 2866Combined sources
Turni291 – 2933Combined sources
Beta strandi299 – 3035Combined sources
Turni304 – 3074Combined sources
Beta strandi308 – 3114Combined sources
Beta strandi323 – 3275Combined sources
Beta strandi330 – 3345Combined sources
Beta strandi346 – 3505Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi373 – 3775Combined sources
Beta strandi380 – 3845Combined sources
Beta strandi395 – 4006Combined sources
Turni401 – 4044Combined sources
Beta strandi405 – 4117Combined sources
Beta strandi420 – 4245Combined sources
Beta strandi427 – 4315Combined sources
Beta strandi443 – 4464Combined sources
Turni448 – 4503Combined sources
Beta strandi453 – 4564Combined sources
Beta strandi467 – 4715Combined sources
Beta strandi474 – 4785Combined sources
Beta strandi483 – 4864Combined sources
Beta strandi490 – 4945Combined sources
Turni495 – 4984Combined sources
Beta strandi499 – 5035Combined sources
Beta strandi514 – 5185Combined sources
Beta strandi521 – 5255Combined sources
Beta strandi530 – 54112Combined sources
Turni542 – 5454Combined sources
Beta strandi546 – 55914Combined sources
Beta strandi561 – 5666Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VPJX-ray1.85A268-567[»]
ProteinModelPortaliQ53G59.
SMRiQ53G59. Positions 5-567.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53G59.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 10068BTBPROSITE-ProRule annotationAdd
BLAST
Domaini135 – 236102BACKAdd
BLAST
Repeati282 – 32948Kelch 1Add
BLAST
Repeati331 – 37949Kelch 2Add
BLAST
Repeati380 – 42647Kelch 3Add
BLAST
Repeati427 – 47347Kelch 4Add
BLAST
Repeati475 – 52046Kelch 5Add
BLAST
Repeati522 – 56746Kelch 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni405 – 568164Interaction with DVL3Add
BLAST

Domaini

The BTB domain is required for interaction with CUL3.

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 6 Kelch repeats.Curated

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiNOG73120.
GeneTreeiENSGT00760000118931.
HOGENOMiHOG000230814.
HOVERGENiHBG014286.
InParanoidiQ53G59.
KOiK10450.
OMAiRYDPHTG.
OrthoDBiEOG7HTHGF.
PhylomeDBiQ53G59.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q53G59-1) [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

        10         20         30         40         50
MGGIMAPKDI MTNTHAKSIL NSMNSLRKSN TLCDVTLRVE QKDFPAHRIV
60 70 80 90 100
LAACSDYFCA MFTSELSEKG KPYVDIQGLT ASTMEILLDF VYTETVHVTV
110 120 130 140 150
ENVQELLPAA CLLQLKGVKQ ACCEFLESQL DPSNCLGIRD FAETHNCVDL
160 170 180 190 200
MQAAEVFSQK HFPEVVQHEE FILLSQGEVE KLIKCDEIQV DSEEPVFEAV
210 220 230 240 250
INWVKHAKKE REESLPNLLQ YVRMPLLTPR YITDVIDAEP FIRCSLQCRD
260 270 280 290 300
LVDEAKKFHL RPELRSQMQG PRTRARLGAN EVLLVVGGFG SQQSPIDVVE
310 320 330 340 350
KYDPKTQEWS FLPSITRKRR YVASVSLHDR IYVIGGYDGR SRLSSVECLD
360 370 380 390 400
YTADEDGVWY SVAPMNVRRG LAGATTLGDM IYVSGGFDGS RRHTSMERYD
410 420 430 440 450
PNIDQWSMLG DMQTAREGAG LVVASGVIYC LGGYDGLNIL NSVEKYDPHT
460 470 480 490 500
GHWTNVTPMA TKRSGAGVAL LNDHIYVVGG FDGTAHLSSV EAYNIRTDSW
510 520 530 540 550
TTVTSMTTPR CYVGATVLRG RLYAIAGYDG NSLLSSIECY DPIIDSWEVV
560
TSMGTQRCDA GVCVLREK
Length:568
Mass (Da):63,277
Last modified:May 16, 2006 - v2
Checksum:i4EB1BC33B6351B5D
GO
Isoform 2 (identifier: Q53G59-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDVNKFEASVGFLDVKKFLSTWKLQNPRTHFVLSPHCFM

Show »
Length:606
Mass (Da):67,727
Checksum:i47F91BE5B8ED7C33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221C → R in BAD96792. 1 PublicationCurated
Sequence conflicti197 – 1982FE → LG in BAD96792. 1 PublicationCurated
Sequence conflicti394 – 3941T → A in BAD96792. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721P → L.
Corresponds to variant rs12569087 [ dbSNP | Ensembl ].
VAR_050049

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDVNKFEASVGFLDVKKFLS TWKLQNPRTHFVLSPHCFM in isoform 2. 1 PublicationVSP_042975

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190900 mRNA. Translation: AAG17175.1.
AK027656 mRNA. Translation: BAB55271.1.
AK301791 mRNA. Translation: BAH13554.1.
AK223072 mRNA. Translation: BAD96792.1.
AC096632 Genomic DNA. No translation available.
BC003183 mRNA. Translation: AAH03183.1.
BC004175 mRNA. Translation: AAH04175.1.
CCDSiCCDS1429.1. [Q53G59-1]
RefSeqiNP_067646.1. NM_021633.2. [Q53G59-1]
XP_005245460.1. XM_005245403.1. [Q53G59-2]
UniGeneiHs.706793.

Genome annotation databases

EnsembliENST00000367261; ENSP00000356230; ENSG00000117153. [Q53G59-1]
GeneIDi59349.
KEGGihsa:59349.
UCSCiuc001gyn.1. human. [Q53G59-1]
uc010pqc.1. human. [Q53G59-2]

Polymorphism databases

DMDMi97054498.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190900 mRNA. Translation: AAG17175.1 .
AK027656 mRNA. Translation: BAB55271.1 .
AK301791 mRNA. Translation: BAH13554.1 .
AK223072 mRNA. Translation: BAD96792.1 .
AC096632 Genomic DNA. No translation available.
BC003183 mRNA. Translation: AAH03183.1 .
BC004175 mRNA. Translation: AAH04175.1 .
CCDSi CCDS1429.1. [Q53G59-1 ]
RefSeqi NP_067646.1. NM_021633.2. [Q53G59-1 ]
XP_005245460.1. XM_005245403.1. [Q53G59-2 ]
UniGenei Hs.706793.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VPJ X-ray 1.85 A 268-567 [» ]
ProteinModelPortali Q53G59.
SMRi Q53G59. Positions 5-567.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121890. 30 interactions.
IntActi Q53G59. 21 interactions.
MINTi MINT-1434520.
STRINGi 9606.ENSP00000356230.

PTM databases

PhosphoSitei Q53G59.

Polymorphism databases

DMDMi 97054498.

Proteomic databases

MaxQBi Q53G59.
PaxDbi Q53G59.
PRIDEi Q53G59.

Protocols and materials databases

DNASUi 59349.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367261 ; ENSP00000356230 ; ENSG00000117153 . [Q53G59-1 ]
GeneIDi 59349.
KEGGi hsa:59349.
UCSCi uc001gyn.1. human. [Q53G59-1 ]
uc010pqc.1. human. [Q53G59-2 ]

Organism-specific databases

CTDi 59349.
GeneCardsi GC01M202860.
HGNCi HGNC:19360. KLHL12.
MIMi 614522. gene.
neXtProti NX_Q53G59.
PharmGKBi PA134952416.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73120.
GeneTreei ENSGT00760000118931.
HOGENOMi HOG000230814.
HOVERGENi HBG014286.
InParanoidi Q53G59.
KOi K10450.
OMAi RYDPHTG.
OrthoDBi EOG7HTHGF.
PhylomeDBi Q53G59.
TreeFami TF329218.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_200841. degradation of DVL.

Miscellaneous databases

ChiTaRSi KLHL12. human.
EvolutionaryTracei Q53G59.
GeneWikii KLHL12.
GenomeRNAii 59349.
NextBioi 65257.
PROi Q53G59.
SOURCEi Search...

Gene expression databases

Bgeei Q53G59.
CleanExi HS_KLHL12.
ExpressionAtlasi Q53G59. baseline and differential.
Genevestigatori Q53G59.

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. "Sequence of a novel kelch-like protein, C3IP1."
    Du M., Zu Z., Liou J.-Y., Chu K.-Y., Sansores Garcia L., Yeh E., Wu K.K.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] (ISOFORMS 1 AND 2).
    Tissue: Teratocarcinoma, Testis and Thyroid.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Kidney adenocarcinoma.
  6. "hDKIR, a human homologue of the Drosophila kelch protein, involved in a ring-like structure."
    Mai A., Jung S.K., Yonehara S.
    Exp. Cell Res. 300:72-83(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH KLHL2.
  7. Cited for: TISSUE SPECIFICITY.
  8. "The KLHL12-cullin-3 ubiquitin ligase negatively regulates the Wnt-beta-catenin pathway by targeting Dishevelled for degradation."
    Angers S., Thorpe C.J., Biechele T.L., Goldenberg S.J., Zheng N., Maccoss M.J., Moon R.T.
    Nat. Cell Biol. 8:348-357(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL3 AND DVL3.
  9. "BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by a Cul3-based E3 ligase."
    Rondou P., Haegeman G., Vanhoenacker P., Van Craenenbroeck K.
    J. Biol. Chem. 283:11083-11096(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DRD4.
  10. "KLHL12-mediated ubiquitination of the dopamine D4 receptor does not target the receptor for degradation."
    Rondou P., Skieterska K., Packeu A., Lintermans B., Vanhoenacker P., Vauquelin G., Haegeman G., Van Craenenbroeck K.
    Cell. Signal. 22:900-913(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Ubiquitin-dependent regulation of COPII coat size and function."
    Jin L., Pahuja K.B., Wickliffe K.E., Gorur A., Baumgartel C., Schekman R., Rape M.
    Nature 482:495-500(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BCR(KLHL12) COMPLEX, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SEC31A, MUTAGENESIS OF 289-PHE-GLY-290.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 268-567.

Entry informationi

Entry nameiKLH12_HUMAN
AccessioniPrimary (citable) accession number: Q53G59
Secondary accession number(s): A6NEN8, B7Z7B8, Q9HBX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: November 26, 2014
This is version 96 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3