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Q9NXV2 (KCTD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BTB/POZ domain-containing protein KCTD5
Gene names
Name:KCTD5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex. Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4. Ref.6

Subunit structure

Homopentamer. Interacts (via C-terminus) with GRASP55/GORASP2. Interacts with CUL3 and with ubiquitinated proteins. Interacts with adeno-associated virus 2 (AAV-2) REP proteins. Ref.1 Ref.6 Ref.9

Subcellular location

Cytoplasmcytosol. Nucleus. Note: Predominantly cytoplasmic, translocated to the nucleus upon interaction with Rep proteins. Ref.1 Ref.6

Induction

Up-regulated in peripheral blood lymphocytes stimulated through the T-cell receptor. Ref.6

Domain

The BTB (POZ) domain is atypical and mediates the formation of a homopentamer instead of a homotetramer. Homopentamerization is due to the presence of 4 residues in the BTB (POZ) domain: Leu-56, Gly-100, Val-112 and Ala-118. Ref.9

Sequence similarities

Contains 1 BTB (POZ) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 234233BTB/POZ domain-containing protein KCTD5
PRO_0000191291

Regions

Domain44 – 146103BTB

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.7
Modified residue101Phosphoserine Ref.7

Experimental info

Sequence conflict1781G → R Ref.1

Secondary structure

.............................. 234
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NXV2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 22097CF5F41CD43D

FASTA23426,093
        10         20         30         40         50         60 
MAENHCELLS PARGGIGAGL GGGLCRRCSA GLGALAQRPG SVSKWVRLNV GGTYFLTTRQ 

        70         80         90        100        110        120 
TLCRDPKSFL YRLCQADPDL DSDKDETGAY LIDRDPTYFG PVLNYLRHGK LVINKDLAEE 

       130        140        150        160        170        180 
GVLEEAEFYN ITSLIKLVKD KIRERDSKTS QVPVKHVYRV LQCQEEELTQ MVSTMSDGWK 

       190        200        210        220        230 
FEQLVSIGSS YNYGNEDQAE FLCVVSKELH NTPYGTASEP SEKAKILQER GSRM 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a cytoplasmic interaction partner of the large regulatory proteins Rep78/Rep68 of adeno-associated virus type 2 (AAV-2)."
Weger S., Hammer E., Goetz A., Heilbronn R.
Virology 362:192-206(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH AAV-S REP.
[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. 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: Colon.
[3]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].
[4]"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].
Tissue: Lymph.
[5]Bienvenut W.V., Heiserich L., Gottlieb E.
Submitted (OCT-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13 AND 48-59, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[6]"KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligases."
Bayon Y., Trinidad A.G., de la Puerta M.L., Del Carmen Rodriguez M., Bogetz J., Rojas A., De Pereda J.M., Rahmouni S., Williams S., Matsuzawa S., Reed J.C., Crespo M.S., Mustelin T., Alonso A.
FEBS J. 275:3900-3910(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CUL3, INDUCTION.
[7]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Pentameric assembly of potassium channel tetramerization domain-containing protein 5."
Dementieva I.S., Tereshko V., McCrossan Z.A., Solomaha E., Araki D., Xu C., Grigorieff N., Goldstein S.A.
J. Mol. Biol. 387:175-191(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 34-234, SUBUNIT, DOMAIN BTB, INTERACTION WITH GORASP2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000047 mRNA. Translation: BAA90906.1.
CH471112 Genomic DNA. Translation: EAW85489.1.
CH471112 Genomic DNA. Translation: EAW85491.1.
BC007314 mRNA. Translation: AAH07314.1.
CCDSCCDS10475.1.
RefSeqNP_061865.1. NM_018992.3.
UniGeneHs.61960.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DRXX-ray3.11A/B/C/D/E34-234[»]
3DRYX-ray3.30A/B/C/D/E34-234[»]
3DRZX-ray1.90A/B/C/D/E40-145[»]
ProteinModelPortalQ9NXV2.
SMRQ9NXV2. Positions 35-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119958. 18 interactions.
IntActQ9NXV2. 7 interactions.
STRING9606.ENSP00000301738.

PTM databases

PhosphoSiteQ9NXV2.

Polymorphism databases

DMDM50401182.

Proteomic databases

MaxQBQ9NXV2.
PaxDbQ9NXV2.
PRIDEQ9NXV2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301738; ENSP00000301738; ENSG00000167977.
GeneID54442.
KEGGhsa:54442.
UCSCuc002crd.3. human.

Organism-specific databases

CTD54442.
GeneCardsGC16P002732.
HGNCHGNC:21423. KCTD5.
MIM611285. gene.
neXtProtNX_Q9NXV2.
PharmGKBPA134923177.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267996.
HOGENOMHOG000231167.
HOVERGENHBG053302.
InParanoidQ9NXV2.
OMAFINSRKS.
OrthoDBEOG7JDQZF.
PhylomeDBQ9NXV2.
TreeFamTF313754.

Gene expression databases

ArrayExpressQ9NXV2.
BgeeQ9NXV2.
GenevestigatorQ9NXV2.

Family and domain databases

Gene3D3.30.710.10. 1 hit.
InterProIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR003131. T1-type_BTB.
[Graphical view]
PfamPF02214. BTB_2. 1 hit.
[Graphical view]
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

ChiTaRSKCTD5. human.
EvolutionaryTraceQ9NXV2.
GenomeRNAi54442.
NextBio56673.
PROQ9NXV2.
SOURCESearch...

Entry information

Entry nameKCTD5_HUMAN
AccessionPrimary (citable) accession number: Q9NXV2
Secondary accession number(s): D3DU96
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 99 of the entry and version 1 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

MIM cross-references

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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM