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Q13829 (BACD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2

Short name=hBACURD2
Alternative name(s):
BTB/POZ domain-containing protein TNFAIP1
Protein B12
Tumor necrosis factor, alpha-induced protein 1, endothelial
Gene names
Name:TNFAIP1
Synonyms:BACURD2, EDP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(BACURD2) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. May enhance the PCNA-dependent DNA polymerase delta activity. Ref.10 Ref.12

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of the BCR(BACURD2) E3 ubiquitin ligase complex, at least composed of CUL3, TNFAIP1/BACURD2 and RBX1. Interacts with RHOA; with a preference for RhoA-GDP. Interacts with RHOB. Interacts with PCNA. Interacts with CSNK2B. Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleus. Endosome. Note: Colocalizes with RHOB in endosomes. Ref.10 Ref.11

Induction

By TNF, IL1B/interleukin-1 beta and bacterial lipopolysaccharides (LPS).

Post-translational modification

Phosphorylation at Ser-280 by CK2 facilitates the nucleus localization and increases interaction with PCNA.

Sequence similarities

Belongs to the BACURD family.

Contains 1 BTB (POZ) domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Endosome
Nucleus
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Traceable author statement Ref.10. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.12. Source: UniProtKB

embryo development

Inferred from sequence or structural similarity. Source: UniProtKB

immune response

Inferred from expression pattern Ref.1. Source: UniProtKB

negative regulation of Rho protein signal transduction

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.12. Source: UniProtKB

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

protein ubiquitination

Inferred from direct assay Ref.12. Source: UniProtKB

stress fiber assembly

Inferred from mutant phenotype Ref.12. Source: UniProtKB

   Cellular_componentCul3-RING ubiquitin ligase complex

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

endosome

Inferred from direct assay Ref.10. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

   Molecular_functionGTP-Rho binding

Inferred from direct assay Ref.10Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RHOBP627455EBI-2505861,EBI-602647

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
PRO_0000191300

Regions

Domain28 – 9669BTB

Amino acid modifications

Modified residue2781Phosphoserine Ref.9 Ref.13
Modified residue2801Phosphoserine; by CK2 Ref.9 Ref.11

Experimental info

Mutagenesis71 – 733ILI → AAA: Abolishes interaction with CUL3 and induces abnormal actin stress fibers. Ref.12
Mutagenesis1421S → A: Does not affect phosphorylation level; when associated with A-237. Ref.11
Mutagenesis2371T → A: Does not affect phosphorylation level; when associated with A-142. Ref.11
Mutagenesis2651S → A: Does not affect phosphorylation level. Ref.11
Mutagenesis2781S → A: Slightly impairs phosphorylation level. Ref.11
Mutagenesis2801S → A: Strongly impairs phosphorylation level. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Q13829 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D20B810A00507DCF

FASTA31636,204
        10         20         30         40         50         60 
MSGDTCLCPA SGAKPKLSGF KGGGLGNKYV QLNVGGSLYY TTVRALTRHD TMLKAMFSGR 

        70         80         90        100        110        120 
MEVLTDKEGW ILIDRCGKHF GTILNYLRDD TITLPQNRQE IKELMAEAKY YLIQGLVNMC 

       130        140        150        160        170        180 
QSALQDKKDS YQPVCNIPII TSLKEEERLI ESSTKPVVKL LYNRSNNKYS YTSNSDDHLL 

       190        200        210        220        230        240 
KNIELFDKLS LRFNGRVLFI KDVIGDEICC WSFYGQGRKL AEVCCTSIVY ATEKKQTKVE 

       250        260        270        280        290        300 
FPEARIYEET LNVLLYETPR VPDNSLLEAT SRSRSQASPS EDEETFELRD RVRRIHVKRY 

       310 
STYDDRQLGH QSTHRD 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a novel tumor necrosis factor-alpha-induced endothelial primary response gene."
Wolf F.W., Marks R.M., Sarma V., Byers M.G., Katz R.W., Shows T.B., Dixit V.M.
J. Biol. Chem. 267:1317-1326(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endothelial cell.
[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: Amygdala.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]SeattleSNPs variation discovery resource
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: Lung.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"RhoB induces apoptosis via direct interaction with TNFAIP1 in HeLa cells."
Kim D.M., Chung K.S., Choi S.J., Jung Y.J., Park S.K., Han G.H., Ha J.S., Song K.B., Choi N.S., Kim H.M., Won M., Seo Y.S.
Int. J. Cancer 125:2520-2527(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RHOB.
[11]"CK2 phosphorylates TNFAIP1 to affect its subcellular localization and interaction with PCNA."
Yang L., Liu N., Hu X., Zhang W., Wang T., Li H., Zhang B., Xiang S., Zhou J., Zhang J.
Mol. Biol. Rep. 37:2967-2973(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSNK2B AND PCNA, PHOSPHORYLATION AT SER-280, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-142; THR-237; SER-265; SER-278 AND SER-280.
[12]"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 71-ILE--ILE-73.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80783 mRNA. Translation: AAA58385.1.
AK312387 mRNA. Translation: BAG35304.1.
CR456819 mRNA. Translation: CAG33100.1.
BT020121 mRNA. Translation: AAV38924.1.
AY065346 Genomic DNA. Translation: AAL38649.1.
AC002094 Genomic DNA. No translation available.
CH471159 Genomic DNA. Translation: EAW51077.1.
BC001643 mRNA. Translation: AAH01643.1.
BC001949 mRNA. Translation: AAH01949.1.
CCDSCCDS11227.1.
RefSeqNP_066960.1. NM_021137.4.
UniGeneHs.76090.

3D structure databases

ProteinModelPortalQ13829.
SMRQ13829. Positions 27-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112981. 14 interactions.
IntActQ13829. 8 interactions.
MINTMINT-3028741.
STRING9606.ENSP00000226225.

PTM databases

PhosphoSiteQ13829.

Polymorphism databases

DMDM2833248.

Proteomic databases

MaxQBQ13829.
PaxDbQ13829.
PRIDEQ13829.

Protocols and materials databases

DNASU7126.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226225; ENSP00000226225; ENSG00000109079.
ENST00000576850; ENSP00000459080; ENSG00000262447.
GeneID7126.
KEGGhsa:7126.
UCSCuc002hax.2. human.

Organism-specific databases

CTD7126.
GeneCardsGC17P026662.
HGNCHGNC:11894. TNFAIP1.
HPAHPA013333.
HPA014641.
MIM191161. gene.
neXtProtNX_Q13829.
PharmGKBPA36591.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG257745.
HOGENOMHOG000294088.
HOVERGENHBG052219.
InParanoidQ13829.
KOK15074.
OMAEMSGDTC.
PhylomeDBQ13829.
TreeFamTF315649.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ13829.
BgeeQ13829.
CleanExHS_TNFAIP1.
GenevestigatorQ13829.

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.
PROSITEPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTNFAIP1.
GenomeRNAi7126.
NextBio27887.
PROQ13829.
SOURCESearch...

Entry information

Entry nameBACD2_HUMAN
AccessionPrimary (citable) accession number: Q13829
Secondary accession number(s): Q5TZQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 123 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM