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Protein

BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2

Gene

TNFAIP1

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(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.2 Publications

Pathwayi

GO - Molecular functioni

  1. GTP-Rho binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cell migration Source: UniProtKB
  3. DNA replication Source: UniProtKB
  4. embryo development Source: UniProtKB
  5. immune response Source: UniProtKB
  6. negative regulation of Rho protein signal transduction Source: UniProtKB
  7. positive regulation of DNA replication Source: Ensembl
  8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  9. protein homooligomerization Source: InterPro
  10. protein ubiquitination Source: UniProtKB
  11. 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 2
Short name:
hBACURD2
Alternative name(s):
BTB/POZ domain-containing protein TNFAIP1
Protein B12
Tumor necrosis factor, alpha-induced protein 1, endothelial
Gene namesi
Name:TNFAIP1
Synonyms:BACURD2, EDP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11894. TNFAIP1.

Subcellular locationi

Cytoplasm. Nucleus. Endosome
Note: Colocalizes with RHOB in endosomes.

GO - Cellular componenti

  1. Cul3-RING ubiquitin ligase complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. endosome Source: UniProtKB
  4. nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi71 – 733ILI → AAA: Abolishes interaction with CUL3 and induces abnormal actin stress fibers. 1 Publication
Mutagenesisi142 – 1421S → A: Does not affect phosphorylation level; when associated with A-237. 1 Publication
Mutagenesisi237 – 2371T → A: Does not affect phosphorylation level; when associated with A-142. 1 Publication
Mutagenesisi265 – 2651S → A: Does not affect phosphorylation level. 1 Publication
Mutagenesisi278 – 2781S → A: Slightly impairs phosphorylation level. 1 Publication
Mutagenesisi280 – 2801S → A: Strongly impairs phosphorylation level. 1 Publication

Organism-specific databases

PharmGKBiPA36591.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2PRO_0000191300Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei278 – 2781Phosphoserine2 Publications
Modified residuei280 – 2801Phosphoserine; by CK22 Publications

Post-translational modificationi

Phosphorylation at Ser-280 by CK2 facilitates the nucleus localization and increases interaction with PCNA.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13829.
PaxDbiQ13829.
PRIDEiQ13829.

PTM databases

PhosphoSiteiQ13829.

Expressioni

Inductioni

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

Gene expression databases

BgeeiQ13829.
CleanExiHS_TNFAIP1.
ExpressionAtlasiQ13829. baseline and differential.
GenevestigatoriQ13829.

Organism-specific databases

HPAiHPA013333.
HPA014641.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RHOBP627455EBI-2505861,EBI-602647

Protein-protein interaction databases

BioGridi112981. 32 interactions.
IntActiQ13829. 8 interactions.
MINTiMINT-3028741.
STRINGi9606.ENSP00000226225.

Structurei

3D structure databases

ProteinModelPortaliQ13829.
SMRiQ13829. Positions 27-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 9669BTBPROSITE-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.
InParanoidiQ13829.
KOiK15074.
OMAiEMSGDTC.
OrthoDBiEOG7PS1G1.
PhylomeDBiQ13829.
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]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q13829-1) [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
MSGDTCLCPA SGAKPKLSGF KGGGLGNKYV QLNVGGSLYY TTVRALTRHD
60 70 80 90 100
TMLKAMFSGR MEVLTDKEGW ILIDRCGKHF GTILNYLRDD TITLPQNRQE
110 120 130 140 150
IKELMAEAKY YLIQGLVNMC QSALQDKKDS YQPVCNIPII TSLKEEERLI
160 170 180 190 200
ESSTKPVVKL LYNRSNNKYS YTSNSDDHLL KNIELFDKLS LRFNGRVLFI
210 220 230 240 250
KDVIGDEICC WSFYGQGRKL AEVCCTSIVY ATEKKQTKVE FPEARIYEET
260 270 280 290 300
LNVLLYETPR VPDNSLLEAT SRSRSQASPS EDEETFELRD RVRRIHVKRY
310
STYDDRQLGH QSTHRD
Length:316
Mass (Da):36,204
Last modified:November 1, 1996 - v1
Checksum:iD20B810A00507DCF
GO
Isoform 2 (identifier: Q13829-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.

Note: No experimental confirmation available.

Show »
Length:212
Mass (Da):24,709
Checksum:i812B6C0368AA6908
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 104104Missing in isoform 2. 1 PublicationVSP_056029Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80783 mRNA. Translation: AAA58385.1.
AK300584 mRNA. Translation: BAH13310.1.
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.
CCDSiCCDS11227.1. [Q13829-1]
RefSeqiNP_066960.1. NM_021137.4. [Q13829-1]
UniGeneiHs.76090.

Genome annotation databases

EnsembliENST00000226225; ENSP00000226225; ENSG00000109079. [Q13829-1]
ENST00000544907; ENSP00000440749; ENSG00000109079. [Q13829-2]
GeneIDi7126.
KEGGihsa:7126.
UCSCiuc002hax.2. human. [Q13829-1]

Polymorphism databases

DMDMi2833248.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80783 mRNA. Translation: AAA58385.1.
AK300584 mRNA. Translation: BAH13310.1.
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.
CCDSiCCDS11227.1. [Q13829-1]
RefSeqiNP_066960.1. NM_021137.4. [Q13829-1]
UniGeneiHs.76090.

3D structure databases

ProteinModelPortaliQ13829.
SMRiQ13829. Positions 27-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112981. 32 interactions.
IntActiQ13829. 8 interactions.
MINTiMINT-3028741.
STRINGi9606.ENSP00000226225.

PTM databases

PhosphoSiteiQ13829.

Polymorphism databases

DMDMi2833248.

Proteomic databases

MaxQBiQ13829.
PaxDbiQ13829.
PRIDEiQ13829.

Protocols and materials databases

DNASUi7126.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000226225; ENSP00000226225; ENSG00000109079. [Q13829-1]
ENST00000544907; ENSP00000440749; ENSG00000109079. [Q13829-2]
GeneIDi7126.
KEGGihsa:7126.
UCSCiuc002hax.2. human. [Q13829-1]

Organism-specific databases

CTDi7126.
GeneCardsiGC17P026662.
HGNCiHGNC:11894. TNFAIP1.
HPAiHPA013333.
HPA014641.
MIMi191161. gene.
neXtProtiNX_Q13829.
PharmGKBiPA36591.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG257745.
GeneTreeiENSGT00530000063071.
HOGENOMiHOG000294088.
HOVERGENiHBG052219.
InParanoidiQ13829.
KOiK15074.
OMAiEMSGDTC.
OrthoDBiEOG7PS1G1.
PhylomeDBiQ13829.
TreeFamiTF315649.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiTNFAIP1. human.
GeneWikiiTNFAIP1.
GenomeRNAii7126.
NextBioi27887.
PROiQ13829.
SOURCEiSearch...

Gene expression databases

BgeeiQ13829.
CleanExiHS_TNFAIP1.
ExpressionAtlasiQ13829. baseline and differential.
GenevestigatoriQ13829.

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. "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(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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 (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. SeattleSNPs variation discovery resource
    Submitted (NOV-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.
    , 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(2005) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  9. 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(2008) [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(2009) [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(2008) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiBACD2_HUMAN
AccessioniPrimary (citable) accession number: Q13829
Secondary accession number(s): B7Z6M4, Q5TZQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 130 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 17
    Human chromosome 17: 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.