Q9NXV2 (KCTD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
BTB/POZ domain-containing protein KCTD5

Gene names

Name:

KCTD5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Cytoplasm › cytosol. 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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein homooligomerization Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay Ref.6. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 234

233

BTB/POZ domain-containing protein KCTD5

PRO_0000191291

Regions

Domain

44 – 146

103

BTB

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5 Ref.7

Modified residue

10

1

Phosphoserine Ref.7

Experimental info

Sequence conflict

178

1

G → R Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

234

Helix Strand Turn

Details...

Beta strand

45 – 50

6

Beta strand

53 – 58

6

Helix

59 – 62

4

Helix

69 – 74

6

Helix

78 – 83

6

Beta strand

90 – 92

3

Helix

96 – 108

13

Beta strand

115 – 117

3

Helix

119 – 129

11

Helix

132 – 144

13

Turn

146 – 148

3

Beta strand

157 – 163

7

Helix

167 – 173

7

Beta strand

180 – 186

7

Beta strand

201 – 207

7

Sequences

	Sequence		Length	Mass (Da)
	Q9NXV2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 22097CF5F41CD43D	FASTA	234	26,093
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. 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.

IPI

IPI00004506.

RefSeq

NP_061865.1. NM_018992.3.

UniGene

Hs.61960.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DRX	X-ray	3.11	A/B/C/D/E	34-234	[»]
3DRY	X-ray	3.30	A/B/C/D/E	34-234	[»]
3DRZ	X-ray	1.90	A/B/C/D/E	40-145	[»]

ProteinModelPortal

Q9NXV2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NXV2. 7 interactions.

STRING

9606.ENSP00000301738.

PTM databases

PhosphoSite

Q9NXV2.

Polymorphism databases

DMDM

50401182.

Proteomic databases

PaxDb

Q9NXV2.

PRIDE

Q9NXV2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000301738; ENSP00000301738; ENSG00000167977.

GeneID

54442.

KEGG

hsa:54442.

UCSC

uc002crd.3. human.

Organism-specific databases

CTD

54442.

GeneCards

GC16P002732.

HGNC

HGNC:21423. KCTD5.

MIM

611285. gene.

neXtProt

NX_Q9NXV2.

PharmGKB

PA134923177.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG267996.

HOGENOM

HOG000231167.

HOVERGEN

HBG053302.

InParanoid

Q9NXV2.

OMA

DCKTSQV.

OrthoDB

EOG4WQ13F.

PhylomeDB

Q9NXV2.

Gene expression databases

ArrayExpress

Q9NXV2.

Bgee

Q9NXV2.

Genevestigator

Q9NXV2.

GermOnline

ENSG00000167977. Homo sapiens.

Family and domain databases

Gene3D

3.30.710.10. 1 hit.

InterPro

IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR003131. T1-type_BTB.
[Graphical view]

Pfam

PF02214. K_tetra. 1 hit.
[Graphical view]

SMART

SM00225. BTB. 1 hit.
[Graphical view]

SUPFAM

SSF54695. BTB/POZ_fold. 1 hit.

PROSITE

PS50097. BTB. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

KCTD5. human.

EvolutionaryTrace

Q9NXV2.

GenomeRNAi

54442.

NextBio

56673.

SOURCE

Search...

Entry information

Entry name

KCTD5_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.