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Q92481 - AP2B_HUMAN

UniProt

Q92481 - AP2B_HUMAN

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Protein

Transcription factor AP-2-beta

Gene

TFAP2B

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  3. DNA binding Source: UniProtKB
  4. enhancer sequence-specific DNA binding Source: UniProtKB
  5. protein dimerization activity Source: UniProtKB
  6. protein heterodimerization activity Source: UniProtKB
  7. protein homodimerization activity Source: UniProtKB
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  9. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB
  10. RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Source: UniProtKB
  11. RNA polymerase II transcription coactivator activity Source: UniProtKB
  12. RNA polymerase II transcription corepressor activity Source: UniProtKB
  13. sequence-specific DNA binding Source: UniProtKB
  14. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  15. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  16. transcription coactivator activity Source: UniProtKB
  17. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. aorta morphogenesis Source: UniProtKB
  2. calcium ion homeostasis Source: UniProtKB
  3. cellular ammonia homeostasis Source: UniProtKB
  4. cellular creatinine homeostasis Source: UniProtKB
  5. cellular urea homeostasis Source: UniProtKB
  6. collecting duct development Source: UniProtKB
  7. distal tubule development Source: UniProtKB
  8. ductus arteriosus closure Source: UniProtKB
  9. fat cell differentiation Source: UniProtKB
  10. forelimb morphogenesis Source: UniProtKB
  11. glucose homeostasis Source: UniProtKB
  12. glucose metabolic process Source: UniProtKB
  13. hindlimb morphogenesis Source: UniProtKB
  14. kidney development Source: UniProtKB
  15. magnesium ion homeostasis Source: UniProtKB
  16. metanephric nephron development Source: Ensembl
  17. negative regulation of apoptotic process Source: UniProtKB
  18. negative regulation of cell proliferation Source: UniProtKB
  19. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  20. negative regulation of neuron apoptotic process Source: Ensembl
  21. negative regulation of transcription, DNA-templated Source: UniProtKB
  22. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  23. phosphate ion homeostasis Source: UniProtKB
  24. positive regulation of cell proliferation Source: UniProtKB
  25. positive regulation of neuron apoptotic process Source: UniProtKB
  26. positive regulation of transcription, DNA-templated Source: UniProtKB
  27. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  28. positive regulation of urine volume Source: UniProtKB
  29. potassium ion homeostasis Source: UniProtKB
  30. regulation of BMP signaling pathway Source: UniProtKB
  31. regulation of cell differentiation Source: UniProtKB
  32. regulation of insulin secretion Source: UniProtKB
  33. regulation of transcription, DNA-templated Source: HGNC
  34. renal water homeostasis Source: UniProtKB
  35. response to drug Source: Ensembl
  36. response to lithium ion Source: Ensembl
  37. retina layer formation Source: UniProtKB
  38. skin development Source: Ensembl
  39. sodium ion homeostasis Source: UniProtKB
  40. sympathetic nervous system development 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11743. TFAP2B.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Char syndrome2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant disorder characterized by patent ductus arteriosus (PDA), facial dysmorphism and hand anomalies.

See also OMIM:169100
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731P → R in CHAR. 1 Publication
VAR_016977
Natural varianti236 – 2361R → C in CHAR. 1 Publication
VAR_016978
Natural varianti236 – 2361R → S in CHAR. 1 Publication
VAR_016979
Natural varianti275 – 2751A → D in CHAR. 1 Publication
VAR_011318
Natural varianti285 – 2851R → Q in CHAR. 1 Publication
VAR_016980
Natural varianti300 – 3001R → C in CHAR. 1 Publication
VAR_011319

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi169100. phenotype.
Orphaneti46627. Char syndrome.
PharmGKBiPA36460.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Transcription factor AP-2-betaPRO_0000184801Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Sumoylated on Lys-21; which inhibits transcriptional activity.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92481.
PaxDbiQ92481.
PRIDEiQ92481.

PTM databases

PhosphoSiteiQ92481.

Expressioni

Gene expression databases

BgeeiQ92481.
CleanExiHS_TFAP2B.
ExpressionAtlasiQ92481. baseline and differential.
GenevestigatoriQ92481.

Organism-specific databases

HPAiCAB010426.
HPA034683.

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.5 Publications

Protein-protein interaction databases

BioGridi112879. 10 interactions.
IntActiQ92481. 4 interactions.
MINTiMINT-1424146.
STRINGi9606.ENSP00000377265.

Structurei

3D structure databases

ProteinModelPortaliQ92481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 13191Gln/Pro-rich (transactivation domain)Add
BLAST

Sequence similaritiesi

Belongs to the AP-2 family.Curated

Phylogenomic databases

eggNOGiNOG300693.
GeneTreeiENSGT00550000074577.
HOVERGENiHBG002455.
InParanoidiQ92481.
KOiK09176.
OMAiIGHPGME.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ92481.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92481-1) [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
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 MFLNNTTTNR HTSGEGPGSK 
       460
TGDKEEKHRK
Length:460
Mass (Da):50,474
Last modified:July 10, 2007 - v2
Checksum:iA6420EA0C265DDA2
GO
Isoform 2 (identifier: Q92481-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     27-27: E → EMLVHTYSSM

Note: No experimental confirmation available.

Show »
Length:469
Mass (Da):51,524
Checksum:iC4E0DCC428DBF0F8
GO

Sequence cautioni

The sequence CAA64990.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA71047.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB41305.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAC01130.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti258 – 2581S → A in CAA71047. (PubMed:9271117)Curated
Sequence conflicti362 – 46099QLCKE…EKHRK → GNFVKNLRIYWRRTGHR in CAA71047. (PubMed:9271117)CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731P → R in CHAR. 1 Publication
VAR_016977
Natural varianti236 – 2361R → C in CHAR. 1 Publication
VAR_016978
Natural varianti236 – 2361R → S in CHAR. 1 Publication
VAR_016979
Natural varianti275 – 2751A → D in CHAR. 1 Publication
VAR_011318
Natural varianti285 – 2851R → Q in CHAR. 1 Publication
VAR_016980
Natural varianti300 – 3001R → C in CHAR. 1 Publication
VAR_011319

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei27 – 271E → EMLVHTYSSM in isoform 2. CuratedVSP_006408

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09912 Genomic DNA. Translation: CAA71047.1. Different initiation.
AL031224 Genomic DNA. Translation: CAB41305.1. Different initiation.
AL031224, AL049693 Genomic DNA. Translation: CAI20235.2.
AL049693 Genomic DNA. Translation: CAB89563.3.
BC037225 mRNA. Translation: AAH37225.2.
AJ278356 Genomic DNA. Translation: CAC01130.1. Different initiation.
X95694 mRNA. Translation: CAA64990.1. Different initiation.
CCDSiCCDS4934.2. [Q92481-1]
RefSeqiNP_003212.2. NM_003221.3. [Q92481-1]
UniGeneiHs.33102.

Genome annotation databases

EnsembliENST00000393655; ENSP00000377265; ENSG00000008196. [Q92481-1]
GeneIDi7021.
KEGGihsa:7021.
UCSCiuc003pag.3. human. [Q92481-1]

Polymorphism databases

DMDMi152031557.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Activatin protein 2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09912 Genomic DNA. Translation: CAA71047.1. Different initiation.
AL031224 Genomic DNA. Translation: CAB41305.1. Different initiation.
AL031224, AL049693 Genomic DNA. Translation: CAI20235.2.
AL049693 Genomic DNA. Translation: CAB89563.3.
BC037225 mRNA. Translation: AAH37225.2.
AJ278356 Genomic DNA. Translation: CAC01130.1. Different initiation.
X95694 mRNA. Translation: CAA64990.1. Different initiation.
CCDSiCCDS4934.2. [Q92481-1]
RefSeqiNP_003212.2. NM_003221.3. [Q92481-1]
UniGeneiHs.33102.

3D structure databases

ProteinModelPortaliQ92481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112879. 10 interactions.
IntActiQ92481. 4 interactions.
MINTiMINT-1424146.
STRINGi9606.ENSP00000377265.

PTM databases

PhosphoSiteiQ92481.

Polymorphism databases

DMDMi152031557.

Proteomic databases

MaxQBiQ92481.
PaxDbiQ92481.
PRIDEiQ92481.

Protocols and materials databases

DNASUi7021.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393655; ENSP00000377265; ENSG00000008196. [Q92481-1]
GeneIDi7021.
KEGGihsa:7021.
UCSCiuc003pag.3. human. [Q92481-1]

Organism-specific databases

CTDi7021.
GeneCardsiGC06P050833.
GeneReviewsiTFAP2B.
HGNCiHGNC:11743. TFAP2B.
HPAiCAB010426.
HPA034683.
MIMi169100. phenotype.
601601. gene.
neXtProtiNX_Q92481.
Orphaneti46627. Char syndrome.
PharmGKBiPA36460.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300693.
GeneTreeiENSGT00550000074577.
HOVERGENiHBG002455.
InParanoidiQ92481.
KOiK09176.
OMAiIGHPGME.
OrthoDBiEOG7HHWS1.
PhylomeDBiQ92481.
TreeFamiTF313718.

Miscellaneous databases

GeneWikiiTFAP2B.
GenomeRNAii7021.
NextBioi27431.
PROiQ92481.
SOURCEiSearch...

Gene expression databases

BgeeiQ92481.
CleanExiHS_TFAP2B.
ExpressionAtlasiQ92481. baseline and differential.
GenevestigatoriQ92481.

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. "Enhanced apoptotic cell death of renal epithelial cells in mice lacking transcription factor AP-2beta."
    Moser M., Buettner R.
    Genes Dev. 11:1938-1948(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1).
    Tissue: Skin.
  4. "Characterisation of the human AP-2beta and AP-2gamma genes."
    Hasleton M.D., Skinner A., Hurst H.C.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
  5. "Chromosomal mapping of the human and mouse homologues of two new members of the AP-2 family of transcription factors."
    Williamson J.A., Bosher J.M., Skinner A., Sheer D., Williams T., Hurst H.C.
    Genomics 35:262-264(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-460 (ISOFORM 1).
    Tissue: Mammary tumor.
  6. "Cardiac malformations, adrenal agenesis, neural crest defects and exencephaly in mice lacking Cited2, a new Tfap2 co-activator."
    Bamforth S.D., Braganca J., Eloranta J.J., Murdoch J.N., Marques F.I., Kranc K.R., Farza H., Henderson D.J., Hurst H.C., Bhattacharya S.
    Nat. Genet. 29:469-474(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CITED2.
  7. "Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2."
    Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J., Hurst H.C., Shioda T., Bhattacharya S.
    J. Biol. Chem. 277:8559-8565(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED4.
  8. "Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo."
    Eloranta J.J., Hurst H.C.
    J. Biol. Chem. 277:30798-30804(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE2I, SUMOYLATION AT LYS-21.
  9. "Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2."
    Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C., Bhattacharya S.
    J. Biol. Chem. 278:16021-16029(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CITED2.
  10. "The interaction of KCTD1 with transcription factor AP-2alpha inhibits its transactivation."
    Ding X., Luo C., Zhou J., Zhong Y., Hu X., Zhou F., Ren K., Gan L., He A., Zhu J., Gao X., Zhang J.
    J. Cell. Biochem. 106:285-295(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCTD1.
  11. "Mutations in TFAP2B cause Char syndrome, a familial form of patent ductus arteriosus."
    Satoda M., Zhao F., Diaz G.A., Burn J., Goodship J., Davidson H.R., Pierpont M.E.M., Gelb B.D.
    Nat. Genet. 25:42-46(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHAR ASP-275 AND CYS-300.
  12. "Novel TFAP2B mutations that cause Char syndrome provide a genotype-phenotype correlation."
    Zhao F., Weismann C.G., Satoda M., Pierpont M.E.M., Sweeney E., Thompson E.M., Gelb B.D.
    Am. J. Hum. Genet. 69:695-703(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CHAR ARG-73; CYS-236; SER-236 AND GLN-285.
+Additional computationally mapped references.

Entry informationi

Entry nameiAP2B_HUMAN
AccessioniPrimary (citable) accession number: Q92481
Secondary accession number(s): Q5JYX6
, Q9NQ63, Q9NU99, Q9UJI7, Q9Y214, Q9Y3K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 10, 2007
Last modified: January 7, 2015
This is version 140 of the entry and version 2 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.