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Protein

Transcription factor AP-2-beta

Gene

Tfap2b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-beta appears to be required for normal face and limb development and for proper terminal differentiation and function of renal tubular epithelia.

GO - Molecular functioni

GO - Biological processi

  • aorta morphogenesis Source: UniProtKB
  • apoptotic process Source: GOC
  • calcium ion homeostasis Source: UniProtKB
  • cellular ammonia homeostasis Source: UniProtKB
  • cellular creatinine homeostasis Source: UniProtKB
  • cellular urea homeostasis Source: UniProtKB
  • collecting duct development Source: UniProtKB
  • distal tubule development Source: UniProtKB
  • ductus arteriosus closure Source: UniProtKB
  • fat cell differentiation Source: UniProtKB
  • forelimb morphogenesis Source: UniProtKB
  • glucose homeostasis Source: UniProtKB
  • glucose metabolic process Source: UniProtKB
  • hindlimb morphogenesis Source: UniProtKB
  • kidney development Source: MGI
  • magnesium ion homeostasis Source: UniProtKB
  • metanephric nephron development Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • phosphate ion homeostasis Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of neuron apoptotic process Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of urine volume Source: UniProtKB
  • potassium ion homeostasis Source: UniProtKB
  • regulation of BMP signaling pathway Source: UniProtKB
  • regulation of cell differentiation Source: UniProtKB
  • regulation of insulin secretion Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • renal water homeostasis Source: UniProtKB
  • response to drug Source: Ensembl
  • response to lithium ion Source: Ensembl
  • retina layer formation Source: Ensembl
  • sensory organ development Source: UniProtKB
  • skin development Source: UniProtKB
  • sodium ion homeostasis Source: UniProtKB
  • sympathetic nervous system development Source: MGI
  • transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor AP-2-beta
Short name:
AP2-beta
Alternative name(s):
Activating enhancer-binding protein 2-beta
Gene namesi
Name:Tfap2b
Synonyms:Tcfap2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:104672. Tfap2b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Transcription factor AP-2-betaPRO_0000184802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki21 – 21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei258 – 2581Phosphoserine; by PKABy similarity

Post-translational modificationi

Sumoylated on Lys-21; which inhibits transcriptional activity.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ61313.
PRIDEiQ61313.

PTM databases

PhosphoSiteiQ61313.

Expressioni

Developmental stagei

Expressed from embryo day 9.5 to birth. In day 13.5 embryo, expressed abundantly in cells coating the neural tube. Expression continues posteriorly in the spinal cord, the dorsal root ganglia, in the prevertebal sympathic ganglia and the ganglion nodosum. High expression found in the dorsal and anteriolateral primordium of the midbrain. Expression also found in skin, kidneys and in many areas of the facial mesenchyme. In adults, expressed in the eye, skin, kidney, prostate, thymus, skeletal muscle and, very weakly in the brain. Highest levels found in kidney.

Inductioni

During retinoic acid-mediated differentiation.

Gene expression databases

BgeeiQ61313.
CleanExiMM_TCFAP2B.
ExpressionAtlasiQ61313. baseline and differential.
GenevisibleiQ61313. MM.

Interactioni

Subunit structurei

Binds DNA as a dimer. Can form homodimers or heterodimers with other AP-2 family members. Interacts with CITED4. Interacts with UBE2I. Interacts with KCTD1; this interaction represses transcription activation. Interacts with CITED2 (via C-terminus); the interaction stimulates TFAP2B-transcriptional activity (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027059.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni299 – 429131H-S-H (helix-span-helix), dimerizationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 13198Gln/Pro-rich (transactivation domain)Add
BLAST

Sequence similaritiesi

Belongs to the AP-2 family.Curated

Phylogenomic databases

eggNOGiNOG300693.
GeneTreeiENSGT00550000074577.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiQ61313.
KOiK09176.
OMAiIGHPGME.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ61313.
TreeFamiTF313718.

Family and domain databases

InterProiIPR004979. TF_AP2.
IPR008122. TF_AP2_beta.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERiPTHR10812. PTHR10812. 1 hit.
PfamiPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSiPR01750. AP2BTNSCPFCT.
PR01748. AP2TNSCPFCT.

Sequencei

Sequence statusi: Complete.

Q61313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSPPRDQAA IMLWKLVENV KYEDIYEDRH DGVPSHSSRL SQLGSVSQGP
60 70 80 90 100
YSSAPPLSHT PSSDFQPPYF PPPYQPLPYH QSQDPYSHVN DPYSLNPLHQ
110 120 130 140 150
PQQHPWGQRQ RQEVGSEAGS LLPQPRAALP QLSGLDPRRD YHSVRRPDVL
160 170 180 190 200
LHSAHHGLDA GMGDSLSLHG LGHPGMEDVQ SVEDANNSGM NLLDQSVIKK
210 220 230 240 250
VPVPPKSVTS LMMNKDGFLG GMSVNTGEVF CSVPGRLSLL SSTSKYKVTV
260 270 280 290 300
GEVQRRLSPP ECLNASLLGG VLRRAKSKNG GRSLRERLEK IGLNLPAGRR
310 320 330 340 350
KAANVTLLTS LVEGEAVHLA RDFGYICETE FPAKAVSEYL NRQHTDPSDL
360 370 380 390 400
HSRKNMLLAT KQLCKEFTDL LAQDRTPIGN SRPSPILEPG IQSCLTHFSL
410 420 430 440 450
ITHGFGAPAI CAALTALQNY LTEALKGMDK MFLNNTTNRH TSGEGPGSKT

GDKEEKHRK
Length:459
Mass (Da):50,373
Last modified:July 10, 2007 - v2
Checksum:iB1932B329D3D98EE
GO

Sequence cautioni

The sequence CAA55036.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78197 mRNA. Translation: CAA55036.1. Different initiation.
AK017373 mRNA. Translation: BAB30714.2.
CCDSiCCDS14839.1.
PIRiS45112.
RefSeqiNP_033360.2. NM_009334.3.
UniGeneiMm.137021.

Genome annotation databases

EnsembliENSMUST00000027059; ENSMUSP00000027059; ENSMUSG00000025927.
GeneIDi21419.
KEGGimmu:21419.
UCSCiuc007akr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78197 mRNA. Translation: CAA55036.1. Different initiation.
AK017373 mRNA. Translation: BAB30714.2.
CCDSiCCDS14839.1.
PIRiS45112.
RefSeqiNP_033360.2. NM_009334.3.
UniGeneiMm.137021.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027059.

PTM databases

PhosphoSiteiQ61313.

Proteomic databases

MaxQBiQ61313.
PRIDEiQ61313.

Protocols and materials databases

DNASUi21419.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027059; ENSMUSP00000027059; ENSMUSG00000025927.
GeneIDi21419.
KEGGimmu:21419.
UCSCiuc007akr.1. mouse.

Organism-specific databases

CTDi7021.
MGIiMGI:104672. Tfap2b.

Phylogenomic databases

eggNOGiNOG300693.
GeneTreeiENSGT00550000074577.
HOGENOMiHOG000231737.
HOVERGENiHBG002455.
InParanoidiQ61313.
KOiK09176.
OMAiIGHPGME.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ61313.
TreeFamiTF313718.

Miscellaneous databases

NextBioi300728.
PROiQ61313.
SOURCEiSearch...

Gene expression databases

BgeeiQ61313.
CleanExiMM_TCFAP2B.
ExpressionAtlasiQ61313. baseline and differential.
GenevisibleiQ61313. MM.

Family and domain databases

InterProiIPR004979. TF_AP2.
IPR008122. TF_AP2_beta.
IPR013854. TF_AP2_C.
[Graphical view]
PANTHERiPTHR10812. PTHR10812. 1 hit.
PfamiPF03299. TF_AP-2. 1 hit.
[Graphical view]
PRINTSiPR01750. AP2BTNSCPFCT.
PR01748. AP2TNSCPFCT.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a second AP-2 transcription factor: AP-2 beta."
    Moser M., Imhof A., Pscherer A., Bauer R., Amselgruber W., Sinowatz F., Schule R., Buettner R.
    Development 121:2779-2788(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  3. "Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding transcriptional coactivators: induced expression in mammary epithelial cells."
    Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T., Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S., Shioda T.
    Genomics 80:601-613(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED4.

Entry informationi

Entry nameiAP2B_MOUSE
AccessioniPrimary (citable) accession number: Q61313
Secondary accession number(s): Q8CEP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 10, 2007
Last modified: June 24, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.