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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: 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 binding Source: UniProtKB
  6. protein dimerization activity Source: UniProtKB
  7. protein heterodimerization activity Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  10. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB
  11. RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Source: UniProtKB
  12. RNA polymerase II transcription coactivator activity Source: UniProtKB
  13. RNA polymerase II transcription corepressor activity Source: UniProtKB
  14. sequence-specific DNA binding Source: UniProtKB
  15. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  16. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  17. transcription coactivator activity Source: UniProtKB
  18. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11743. TFAP2B.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Char syndrome (CHAR) [MIM:169100]: An autosomal dominant disorder characterized by patent ductus arteriosus (PDA), facial dysmorphism and hand anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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) Inferred
Modified residuei258 – 2581Phosphoserine; by PKA By similarity

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92481.
PaxDbiQ92481.
PRIDEiQ92481.

PTM databases

PhosphoSiteiQ92481.

Expressioni

Gene expression databases

ArrayExpressiQ92481.
BgeeiQ92481.
CleanExiHS_TFAP2B.
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. 11 interactions.
IntActiQ92481. 4 interactions.
MINTiMINT-1424146.
STRINGi9606.ENSP00000377265.

Structurei

3D structure databases

ProteinModelPortaliQ92481.

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.

Phylogenomic databases

eggNOGiNOG300693.
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

MHSPPRDQAA IMLWKLVENV KYEDIYEDRH DGVPSHSSRL SQLGSVSQGP    50
YSSAPPLSHT PSSDFQPPYF PPPYQPLPYH QSQDPYSHVN DPYSLNPLHQ 100
PQQHPWGQRQ RQEVGSEAGS LLPQPRAALP QLSGLDPRRD YHSVRRPDVL 150
LHSAHHGLDA GMGDSLSLHG LGHPGMEDVQ SVEDANNSGM NLLDQSVIKK 200
VPVPPKSVTS LMMNKDGFLG GMSVNTGEVF CSVPGRLSLL SSTSKYKVTV 250
GEVQRRLSPP ECLNASLLGG VLRRAKSKNG GRSLRERLEK IGLNLPAGRR 300
KAANVTLLTS LVEGEAVHLA RDFGYICETE FPAKAVSEYL NRQHTDPSDL 350
HSRKNMLLAT KQLCKEFTDL LAQDRTPIGN SRPSPILEPG IQSCLTHFSL 400
ITHGFGAPAI CAALTALQNY LTEALKGMDK MFLNNTTTNR HTSGEGPGSK 450
TGDKEEKHRK 460
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.
The sequence CAA71047.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAB41305.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAC01130.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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. VSP_006408

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti258 – 2581S → A in CAA71047. 1 Publication
Sequence conflicti362 – 46099QLCKE…EKHRK → GNFVKNLRIYWRRTGHR in CAA71047. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000263046; ENSP00000263046; ENSG00000008196. [Q92481-2]
ENST00000393655; 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:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS4934.2. [Q92481-1 ]
RefSeqi NP_003212.2. NM_003221.3. [Q92481-1 ]
UniGenei Hs.33102.

3D structure databases

ProteinModelPortali Q92481.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112879. 11 interactions.
IntActi Q92481. 4 interactions.
MINTi MINT-1424146.
STRINGi 9606.ENSP00000377265.

PTM databases

PhosphoSitei Q92481.

Polymorphism databases

DMDMi 152031557.

Proteomic databases

MaxQBi Q92481.
PaxDbi Q92481.
PRIDEi Q92481.

Protocols and materials databases

DNASUi 7021.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263046 ; ENSP00000263046 ; ENSG00000008196 . [Q92481-2 ]
ENST00000393655 ; ENSP00000377265 ; ENSG00000008196 . [Q92481-1 ]
GeneIDi 7021.
KEGGi hsa:7021.
UCSCi uc003pag.3. human. [Q92481-1 ]

Organism-specific databases

CTDi 7021.
GeneCardsi GC06P050833.
GeneReviewsi TFAP2B.
HGNCi HGNC:11743. TFAP2B.
HPAi CAB010426.
HPA034683.
MIMi 169100. phenotype.
601601. gene.
neXtProti NX_Q92481.
Orphaneti 46627. Char syndrome.
PharmGKBi PA36460.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300693.
HOVERGENi HBG002455.
InParanoidi Q92481.
KOi K09176.
OMAi IGHPGME.
OrthoDBi EOG7HHWS1.
PhylomeDBi Q92481.
TreeFami TF313718.

Miscellaneous databases

GeneWikii TFAP2B.
GenomeRNAii 7021.
NextBioi 27431.
PROi Q92481.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92481.
Bgeei Q92481.
CleanExi HS_TFAP2B.
Genevestigatori Q92481.

Family and domain databases

InterProi IPR004979. TF_AP2.
IPR008122. TF_AP2_beta.
IPR013854. TF_AP2_C.
[Graphical view ]
PANTHERi PTHR10812. PTHR10812. 1 hit.
Pfami PF03299. TF_AP-2. 1 hit.
[Graphical view ]
PRINTSi PR01750. AP2BTNSCPFCT.
PR01748. AP2TNSCPFCT.
ProtoNeti Search...

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.

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: July 9, 2014
This is version 137 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