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Protein

BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1

Gene

KCTD13

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

Functioni

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(BACURD1) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration.1 Publication

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • GTP-Rho binding Source: UniProtKB

GO - Biological processi

  • cell migration Source: UniProtKB
  • DNA replication Source: UniProtKB
  • negative regulation of Rho protein signal transduction Source: UniProtKB
  • positive regulation of DNA replication Source: Ensembl
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein homooligomerization Source: InterPro
  • protein ubiquitination Source: UniProtKB
  • stress fiber assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1
Short name:
hBACURD1
Alternative name(s):
BTB/POZ domain-containing protein KCTD13
Polymerase delta-interacting protein 1
TNFAIP1-like protein
Gene namesi
Name:KCTD13
Synonyms:BACURD1, PDIP1, POLDIP1
ORF Names:FKSG86, PP6832
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:22234. KCTD13.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • Cul3-RING ubiquitin ligase complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi84 – 863VLI → AAA: Abolishes interaction with CUL3 and induces abnormal actin stress fibers. 1 Publication

Organism-specific databases

PharmGKBiPA134907908.

Polymorphism and mutation databases

BioMutaiKCTD13.
DMDMi51701604.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 1PRO_0000191297Add
BLAST

Proteomic databases

MaxQBiQ8WZ19.
PaxDbiQ8WZ19.
PRIDEiQ8WZ19.

PTM databases

PhosphoSiteiQ8WZ19.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues.1 Publication

Inductioni

By TNF and IL6/interleukin-6.1 Publication

Gene expression databases

BgeeiQ8WZ19.
CleanExiHS_KCTD13.
ExpressionAtlasiQ8WZ19. baseline and differential.
GenevisibleiQ8WZ19. HS.

Organism-specific databases

HPAiHPA043524.

Interactioni

Subunit structurei

Component of the BCR(BACURD1) E3 ubiquitin ligase complex, at least composed of CUL3, KCTD13/BACURD1 and RBX1. Interacts with RHOA; with a preference for RhoA-GDP. Interacts with POLD2 and PCNA.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL3Q136183EBI-742916,EBI-456129
TNFAIP1Q138294EBI-742916,EBI-2505861
ZMYND19Q96E354EBI-742916,EBI-746595

Protein-protein interaction databases

BioGridi129001. 24 interactions.
IntActiQ8WZ19. 14 interactions.
MINTiMINT-1458356.
STRINGi9606.ENSP00000311202.

Structurei

3D structure databases

ProteinModelPortaliQ8WZ19.
SMRiQ8WZ19. Positions 40-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 10969BTBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the BACURD family.Curated
Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG257745.
GeneTreeiENSGT00530000063071.
HOGENOMiHOG000294088.
HOVERGENiHBG052219.
InParanoidiQ8WZ19.
KOiK15074.
OMAiDEDGREH.
OrthoDBiEOG7PS1G1.
PhylomeDBiQ8WZ19.
TreeFamiTF315649.

Family and domain databases

InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR003131. T1-type_BTB.
[Graphical view]
PfamiPF02214. BTB_2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8WZ19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAEASGPAA AAAPSLEAPK PSGLEPGPAA YGLKPLTPNS KYVKLNVGGS
60 70 80 90 100
LHYTTLRTLT GQDTMLKAMF SGRVEVLTDA GGWVLIDRSG RHFGTILNYL
110 120 130 140 150
RDGSVPLPES TRELGELLGE ARYYLVQGLI EDCQLALQQK RETLSPLCLI
160 170 180 190 200
PMVTSPREEQ QLLASTSKPV VKLLHNRSNN KYSYTSTSDD NLLKNIELFD
210 220 230 240 250
KLALRFHGRL LFLKDVLGDE ICCWSFYGQG RKIAEVCCTS IVYATEKKQT
260 270 280 290 300
KVEFPEARIF EETLNILIYE TPRGPDPALL EATGGAAGAG GAGRGEDEEN
310 320
REHRVRRIHV RRHITHDERP HGQQIVFKD
Length:329
Mass (Da):36,357
Last modified:March 1, 2002 - v1
Checksum:i17A8AC2DBE81EE78
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2511K → N in AAK27301 (Ref. 3) Curated
Sequence conflicti328 – 3281K → R in AAK27301 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF401315 mRNA. Translation: AAL14962.2.
AY027918 mRNA. Translation: AAK27301.1.
AF289573 mRNA. Translation: AAL55757.1.
AK289630 mRNA. Translation: BAF82319.1.
AC120114 Genomic DNA. No translation available.
CH471238 Genomic DNA. Translation: EAW79969.1.
BC036228 mRNA. Translation: AAH36228.1.
CCDSiCCDS10661.1.
RefSeqiNP_849194.1. NM_178863.4.
UniGeneiHs.534590.

Genome annotation databases

EnsembliENST00000308768; ENSP00000311202; ENSG00000174943.
ENST00000568000; ENSP00000455785; ENSG00000174943.
GeneIDi253980.
KEGGihsa:253980.
UCSCiuc002duv.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF401315 mRNA. Translation: AAL14962.2.
AY027918 mRNA. Translation: AAK27301.1.
AF289573 mRNA. Translation: AAL55757.1.
AK289630 mRNA. Translation: BAF82319.1.
AC120114 Genomic DNA. No translation available.
CH471238 Genomic DNA. Translation: EAW79969.1.
BC036228 mRNA. Translation: AAH36228.1.
CCDSiCCDS10661.1.
RefSeqiNP_849194.1. NM_178863.4.
UniGeneiHs.534590.

3D structure databases

ProteinModelPortaliQ8WZ19.
SMRiQ8WZ19. Positions 40-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129001. 24 interactions.
IntActiQ8WZ19. 14 interactions.
MINTiMINT-1458356.
STRINGi9606.ENSP00000311202.

PTM databases

PhosphoSiteiQ8WZ19.

Polymorphism and mutation databases

BioMutaiKCTD13.
DMDMi51701604.

Proteomic databases

MaxQBiQ8WZ19.
PaxDbiQ8WZ19.
PRIDEiQ8WZ19.

Protocols and materials databases

DNASUi253980.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308768; ENSP00000311202; ENSG00000174943.
ENST00000568000; ENSP00000455785; ENSG00000174943.
GeneIDi253980.
KEGGihsa:253980.
UCSCiuc002duv.4. human.

Organism-specific databases

CTDi253980.
GeneCardsiGC16M029922.
HGNCiHGNC:22234. KCTD13.
HPAiHPA043524.
MIMi608947. gene.
neXtProtiNX_Q8WZ19.
PharmGKBiPA134907908.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG257745.
GeneTreeiENSGT00530000063071.
HOGENOMiHOG000294088.
HOVERGENiHBG052219.
InParanoidiQ8WZ19.
KOiK15074.
OMAiDEDGREH.
OrthoDBiEOG7PS1G1.
PhylomeDBiQ8WZ19.
TreeFamiTF315649.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

GeneWikiiKCTD13.
GenomeRNAii253980.
NextBioi92216.
PROiQ8WZ19.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WZ19.
CleanExiHS_KCTD13.
ExpressionAtlasiQ8WZ19. baseline and differential.
GenevisibleiQ8WZ19. HS.

Family and domain databases

InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR003131. T1-type_BTB.
[Graphical view]
PfamiPF02214. BTB_2. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A tumor necrosis factor alpha- and interleukin 6-inducible protein that interacts with the small subunit of DNA polymerase delta and proliferating cell nuclear antigen."
    He H., Tan C.-K., Downey K.M., So A.G.
    Proc. Natl. Acad. Sci. U.S.A. 98:11979-11984(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH PCNA AND POLD2, TISSUE SPECIFICITY, INDUCTION.
  2. He H., Tan C.-K., Downey K.M., So A.G.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Cloning and characterization of FKSG86, a novel gene encoding a TNFAIP1-like protein."
    Wang Y.-G., Gong L.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "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: Amygdala.
  6. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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: Brain.
  9. "Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement."
    Chen Y., Yang Z., Meng M., Zhao Y., Dong N., Yan H., Liu L., Ding M., Peng H.B., Shao F.
    Mol. Cell 35:841-855(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A BCR (BTB-CUL3-RBX1) E3 UBIQUITIN LIGASE COMPLEX, INTERACTION WITH RHOA, MUTAGENESIS OF 84-VAL--ILE-86.

Entry informationi

Entry nameiBACD1_HUMAN
AccessioniPrimary (citable) accession number: Q8WZ19
Secondary accession number(s): A8K0R5, Q96P93, Q96SA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: March 1, 2002
Last modified: June 24, 2015
This is version 111 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.