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Protein

BTB/POZ domain-containing protein KCTD17

Gene

KCTD17

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. It acts as a substrate-adapter for CUL3-RING ubiquitin ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of TCHP, a protein involved in ciliogenesis down-regulation (PubMed:25270598). May be involved in endoplasmic reticulum calcium ion homeostasis (PubMed:25983243).2 Publications

GO - Molecular functioni

  • cullin family protein binding Source: UniProtKB
  • identical protein binding Source: IntAct

GO - Biological processi

  • cell projection organization Source: UniProtKB-KW
  • endoplasmic reticulum calcium ion homeostasis Source: UniProtKB
  • positive regulation of cilium assembly Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein homooligomerization Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
BTB/POZ domain-containing protein KCTD17
Gene namesi
Name:KCTD17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:25705. KCTD17.

Subcellular locationi

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Dystonia 26, myoclonic (DYT26)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of dystonia, a disorder defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT26 is an autosomal dominant, progressive disorder characterized by a combination of non-epileptic myoclonic jerks and dystonia. Affected individuals manifest myoclonic jerks in the upper limbs during the first or second decade of life, and later develop dystonia with predominant involvement of the craniocervical regions and sometimes the trunk and/or lower limbs.
See also OMIM:616398
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451R → H in DYT26; does not affect cytoplasmic subcellular location. 1 Publication
VAR_073806

Keywords - Diseasei

Disease mutation, Dystonia

Organism-specific databases

MIMi616398. phenotype.
PharmGKBiPA142671638.

Polymorphism and mutation databases

DMDMi205371782.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321BTB/POZ domain-containing protein KCTD17PRO_0000247841Add
BLAST

Proteomic databases

EPDiQ8N5Z5.
MaxQBiQ8N5Z5.
PRIDEiQ8N5Z5.

PTM databases

iPTMnetiQ8N5Z5.
PhosphoSiteiQ8N5Z5.

Expressioni

Tissue specificityi

Highly expressed in brain. Highest expression is observed in the putamen and the thalamus.1 Publication

Gene expression databases

BgeeiQ8N5Z5.
CleanExiHS_KCTD17.
ExpressionAtlasiQ8N5Z5. baseline and differential.
GenevisibleiQ8N5Z5. HS.

Organism-specific databases

HPAiHPA017602.
HPA018459.

Interactioni

Subunit structurei

Interacts with TCHP. Interacts with CUL3, as part of the BCR(KCTD17) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD17 and RBX1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-743960,EBI-743960
DMC1Q145653EBI-743960,EBI-930865
STK16O757164EBI-743960,EBI-749295
SUV39H2Q9H5I12EBI-743960,EBI-723127
TINF2Q9BSI42EBI-743960,EBI-717399

GO - Molecular functioni

  • cullin family protein binding Source: UniProtKB
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi122848. 65 interactions.
IntActiQ8N5Z5. 17 interactions.
MINTiMINT-1436480.

Structurei

Secondary structure

1
321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 377Combined sources
Beta strandi40 – 456Combined sources
Helixi46 – 494Combined sources
Helixi56 – 616Combined sources
Beta strandi76 – 783Combined sources
Helixi82 – 843Combined sources
Helixi85 – 9410Combined sources
Helixi105 – 11511Combined sources
Helixi118 – 1269Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5A6RX-ray2.85A/B/C/D/E20-131[»]
ProteinModelPortaliQ8N5Z5.
SMRiQ8N5Z5. Positions 27-197.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 10171BTBAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili203 – 24644Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi258 – 31154Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 BTB (POZ) domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00530000062980.
HOGENOMiHOG000231167.
HOVERGENiHBG108056.
InParanoidiQ8N5Z5.
OMAiGRAMRME.
OrthoDBiEOG7JDQZF.
PhylomeDBiQ8N5Z5.
TreeFamiTF313754.

Family and domain databases

InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
[Graphical view]
PfamiPF02214. BTB_2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N5Z5-1) [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
MQTPRPAMRM EAGEAAPPAG AGGRAAGGWG KWVRLNVGGT VFLTTRQTLC
60 70 80 90 100
REQKSFLSRL CQGEELQSDR DETGAYLIDR DPTYFGPILN FLRHGKLVLD
110 120 130 140 150
KDMAEEGVLE EAEFYNIGPL IRIIKDRMEE KDYTVTQVPP KHVYRVLQCQ
160 170 180 190 200
EEELTQMVST MSDGWRFEQL VNIGSSYNYG SEDQAEFLCV VSKELHSTPN
210 220 230 240 250
GLSSESSRKT KSTEEQLEEQ QQQEEEVEEV EVEQVQVEAD AQEKAQSSQD
260 270 280 290 300
PANLFSLPPL PPPPLPAGGS RPHPLRPEAE LAVRASPRPL ARPQSCHPCC
310 320
YKPEAPGCEA PDHLQGLGVP I
Length:321
Mass (Da):35,670
Last modified:September 2, 2008 - v3
Checksum:iDB80D4B4BD8CB7E7
GO
Isoform 2 (identifier: Q8N5Z5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     245-268: Missing.

Note: No experimental confirmation available.
Show »
Length:297
Mass (Da):33,276
Checksum:iF69D7CFFE51B0FC9
GO

Sequence cautioni

The sequence AAH25403.1 differs from that shown.The sequence differs in the N-terminus for unknown reasons.Curated
The sequence AAH31038.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61P → R in AAH31038 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511R → G.1 Publication
Corresponds to variant rs17852877 [ dbSNP | Ensembl ].
VAR_027157
Natural varianti145 – 1451R → H in DYT26; does not affect cytoplasmic subcellular location. 1 Publication
VAR_073806

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei245 – 26824Missing in isoform 2. 2 PublicationsVSP_020072Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL022314 Genomic DNA. Translation: CAQ07355.1.
AL022314 Genomic DNA. Translation: CAQ07356.1.
CH471095 Genomic DNA. Translation: EAW60139.1.
BC025403 mRNA. Translation: AAH25403.1. Sequence problems.
BC031038 mRNA. Translation: AAH31038.1. Different initiation.
AK022304 mRNA. Translation: BAB14007.1.
CCDSiCCDS13940.2. [Q8N5Z5-2]
CCDS74854.1. [Q8N5Z5-1]
RefSeqiNP_001269613.1. NM_001282684.1. [Q8N5Z5-1]
NP_001269614.1. NM_001282685.1.
NP_001269615.1. NM_001282686.1.
NP_078957.2. NM_024681.3. [Q8N5Z5-2]
UniGeneiHs.517597.

Genome annotation databases

EnsembliENST00000402077; ENSP00000384391; ENSG00000100379. [Q8N5Z5-2]
ENST00000403888; ENSP00000385096; ENSG00000100379. [Q8N5Z5-1]
GeneIDi79734.
KEGGihsa:79734.
UCSCiuc010gxb.5. human. [Q8N5Z5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL022314 Genomic DNA. Translation: CAQ07355.1.
AL022314 Genomic DNA. Translation: CAQ07356.1.
CH471095 Genomic DNA. Translation: EAW60139.1.
BC025403 mRNA. Translation: AAH25403.1. Sequence problems.
BC031038 mRNA. Translation: AAH31038.1. Different initiation.
AK022304 mRNA. Translation: BAB14007.1.
CCDSiCCDS13940.2. [Q8N5Z5-2]
CCDS74854.1. [Q8N5Z5-1]
RefSeqiNP_001269613.1. NM_001282684.1. [Q8N5Z5-1]
NP_001269614.1. NM_001282685.1.
NP_001269615.1. NM_001282686.1.
NP_078957.2. NM_024681.3. [Q8N5Z5-2]
UniGeneiHs.517597.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5A6RX-ray2.85A/B/C/D/E20-131[»]
ProteinModelPortaliQ8N5Z5.
SMRiQ8N5Z5. Positions 27-197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122848. 65 interactions.
IntActiQ8N5Z5. 17 interactions.
MINTiMINT-1436480.

PTM databases

iPTMnetiQ8N5Z5.
PhosphoSiteiQ8N5Z5.

Polymorphism and mutation databases

DMDMi205371782.

Proteomic databases

EPDiQ8N5Z5.
MaxQBiQ8N5Z5.
PRIDEiQ8N5Z5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000402077; ENSP00000384391; ENSG00000100379. [Q8N5Z5-2]
ENST00000403888; ENSP00000385096; ENSG00000100379. [Q8N5Z5-1]
GeneIDi79734.
KEGGihsa:79734.
UCSCiuc010gxb.5. human. [Q8N5Z5-1]

Organism-specific databases

CTDi79734.
GeneCardsiKCTD17.
HGNCiHGNC:25705. KCTD17.
HPAiHPA017602.
HPA018459.
MIMi616386. gene.
616398. phenotype.
neXtProtiNX_Q8N5Z5.
PharmGKBiPA142671638.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000062980.
HOGENOMiHOG000231167.
HOVERGENiHBG108056.
InParanoidiQ8N5Z5.
OMAiGRAMRME.
OrthoDBiEOG7JDQZF.
PhylomeDBiQ8N5Z5.
TreeFamiTF313754.

Miscellaneous databases

GenomeRNAii79734.
NextBioi69122.
PROiQ8N5Z5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N5Z5.
CleanExiHS_KCTD17.
ExpressionAtlasiQ8N5Z5. baseline and differential.
GenevisibleiQ8N5Z5. HS.

Family and domain databases

InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
[Graphical view]
PfamiPF02214. BTB_2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] OF 3-321 (ISOFORMS 1 AND 2), VARIANT GLY-51.
    Tissue: Brain and Testis.
  4. "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] OF 8-321 (ISOFORM 2).
    Tissue: Mammary gland.
  5. "Ubiquitin-proteasome system controls ciliogenesis at the initial step of axoneme extension."
    Kasahara K., Kawakami Y., Kiyono T., Yonemura S., Kawamura Y., Era S., Matsuzaki F., Goshima N., Inagaki M.
    Nat. Commun. 5:5081-5081(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TCHP AND CUL3, SUBUNIT.
  6. Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN DYT26, VARIANT DYT26 HIS-145, CHARACTERIZATION OF VARIANT DYT26 HIS-145.

Entry informationi

Entry nameiKCD17_HUMAN
AccessioniPrimary (citable) accession number: Q8N5Z5
Secondary accession number(s): B0QYA9, B0QYB0, O95517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: September 2, 2008
Last modified: March 16, 2016
This is version 104 of the entry and version 3 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 22
    Human chromosome 22: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.