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O00213 (APBB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amyloid beta A4 precursor protein-binding family B member 1
Alternative name(s):
Protein Fe65
Gene names
Name:APBB1
Synonyms:FE65, RIR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length710 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its trancription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s). Ref.9 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

Component of a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts (via PID domain 2) with APP (with the intracellular domain of the beta-amyloid precursor protein). Interacts (via PID domain 2) with RASD1/DEXRAS1; impairs the trancription activation activity. Interacts (via PID domain 1) with KAT5/TIP60. Interacts (via the WW domain) with the proline-rich region of APBB1IP. Interacts with TSHZ1 and TSHZ2 By similarity. Interacts (via the WW domain) with histone H2AX (when phosphorylated on 'Tyr-142') and the proline-rich region of ENAH. Interacts with MAPK8. Interacts (via PID domain 1) with TSHZ3 (via homeobox domain). Interacts with SET. Found in a trimeric complex with HDAC1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Interacts (via WWW domain) with NEK6. Interacts (via WWW domain) with ABL1. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Cell membrane. Cytoplasm. Nucleus. Cell projectiongrowth cone By similarity. Nucleus speckle. Note: Colocalizes with TSHZ3 in axonal growth cone By similarity. In normal conditions, it mainly localizes to the cytoplasm, while a small fraction is tethered to the cell membrane via its interaction with APP. Following exposure to DNA damaging agents, it is released from cell membrane and translocates to the nucleus. Nuclear translocation is under the regulation of APP. Colocalizes with TSHZ3 in the nucleus. Colocalizes with NEK6 at the nuclear speckles. Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus By similarity. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14

Tissue specificity

Highly expressed in brain; strongly reduced in post-mortem elderly subjects with Alzheimer disease. Ref.14

Post-translational modification

Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus By similarity. Phosphorylated following nuclear translocation. Phosphorylation at Tyr-547 by ABL1 enhances transcriptional activation activity and reduces the affinity for RASD1/DEXRAS1. Ref.9 Ref.12

Sequence similarities

Contains 2 PID domains.

Contains 1 WW domain.

Sequence caution

The sequence CAD98057.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
DNA damage
Transcription
Transcription regulation
   Cellular componentCell membrane
Cell projection
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionActivator
Chromatin regulator
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Non-traceable author statement PubMed 12843239. Source: UniProtKB

cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay Ref.11. Source: UniProtKB

double-strand break repair

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

histone H4 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of thymidylate synthase biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

neuron migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA repair

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Non-traceable author statement Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

growth cone

Inferred from direct assay PubMed 12843239. Source: UniProtKB

lamellipodium

Inferred from direct assay PubMed 12843239. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.11Ref.14. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

synapse

Inferred from direct assay PubMed 12843239. Source: UniProtKB

   Molecular_functionbeta-amyloid binding

Inferred from physical interaction Ref.11. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.14. Source: UniProtKB

histone binding

Inferred from physical interaction Ref.13. Source: UniProtKB

proline-rich region binding

Inferred from physical interaction Ref.15. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13Ref.14. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00213-1)

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.
Isoform 2 (identifier: O00213-2)

The sequence of this isoform differs from the canonical sequence as follows:
     462-463: Missing.
Isoform 3 (identifier: O00213-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-213: Missing.
     214-240: NSAASDEDSSWATLSQGSPSYGSPEDT → MSAMFSQDFFLAIILQDSSA
     462-463: Missing.
Isoform 4 (identifier: O00213-4)

Also known as: p60Fe65;

The sequence of this isoform differs from the canonical sequence as follows:
     1-259: Missing.
Note: Expressed preferentially in the brain.
Isoform 5 (identifier: O00213-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-213: Missing.
     214-240: NSAASDEDSSWATLSQGSPSYGSPEDT → MSAMFSQDFFLAIILQDSSA
Note: No experimental confirmation available.
Isoform 6 (identifier: O00213-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-240: MSVPSSLSQS...SPSYGSPEDT → MTQMR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 710710Amyloid beta A4 precursor protein-binding family B member 1
PRO_0000076049

Regions

Domain253 – 28533WW
Domain370 – 509140PID 1
Domain542 – 699158PID 2
Compositional bias158 – 17114Glu-rich

Amino acid modifications

Modified residue5471Phosphotyrosine; by ABL1 Ref.9 Ref.12
Modified residue6101Phosphoserine; by SGK1 By similarity

Natural variations

Alternative sequence1 – 259259Missing in isoform 4.
VSP_047459
Alternative sequence1 – 240240MSVPS…SPEDT → MTQMR in isoform 6.
VSP_054709
Alternative sequence1 – 213213Missing in isoform 3 and isoform 5.
VSP_045326
Alternative sequence214 – 24027NSAAS…SPEDT → MSAMFSQDFFLAIILQDSSA in isoform 3 and isoform 5.
VSP_045327
Alternative sequence462 – 4632Missing in isoform 2 and isoform 3.
VSP_011658
Natural variant3271M → V.
Corresponds to variant rs1800423 [ dbSNP | Ensembl ].
VAR_014444
Natural variant3961N → S.
Corresponds to variant rs1800425 [ dbSNP | Ensembl ].
VAR_014445

Experimental info

Mutagenesis1171Y → F: No effect on phosphorylation by ABL1. Ref.9
Mutagenesis2341Y → F: No effect on phosphorylation by ABL1. Ref.9
Mutagenesis269 – 2713YYW → AAA: Impairs transcriptional activation and inhibits binding to ABL1. Ref.9
Mutagenesis2691Y → F: No effect on phosphorylation by ABL1. Ref.9
Mutagenesis2701Y → F: No effect on phosphorylation by ABL1. Ref.9
Mutagenesis4031Y → F: No effect on phosphorylation by ABL1. Ref.9
Mutagenesis4671Y → F: No effect on phosphorylation by ABL1. Ref.9
Mutagenesis5461Y → F: No effect on phosphorylation by ABL1. Ref.9
Mutagenesis5471Y → F: Abrogates phosphorylation and stimulation of transcription by ABL1, and increases the interaction with RASD1/DEXRAS1. Ref.9 Ref.12
Mutagenesis6581Y → F: No effect on phosphorylation by ABL1.
Sequence conflict3671I → T in BAH11532. Ref.4
Sequence conflict4931T → A in BAH11532. Ref.4

Secondary structure

......................................................... 710
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: FD4A2EF7E8D8E884

FASTA71077,244
        10         20         30         40         50         60 
MSVPSSLSQS AINANSHGGP ALSLPLPLHA AHNQLLNAKL QATAVGPKDL RSAMGEGGGP 

        70         80         90        100        110        120 
EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS QEPEMAPLGP KGLIHLYSEL 

       130        140        150        160        170        180 
ELSAHNAANR GLRGPGLIIS TQEQGPDEGE EKAAGEAEEE EEDDDDEEEE EDLSSPPGLP 

       190        200        210        220        230        240 
EPLESVEAPP RPQALTDGPR EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT 

       250        260        270        280        290        300 
DSFWNPNAFE TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL 

       310        320        330        340        350        360 
TWTGFAHGEG FEDGEFWKDE PSDEAPMELG LKEPEEGTLT FPAQSLSPEP LPQEEEKLPP 

       370        380        390        400        410        420 
RNTNPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ LSYHKNNLHD PMSGGWGEGK 

       430        440        450        460        470        480 
DLLLQLEDET LKLVEPQSQA LLHAQPIISI RVWGVGRDSG RERDFAYVAR DKLTQMLKCH 

       490        500        510        520        530        540 
VFRCEAPAKN IATSLHEICS KIMAERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV 

       550        560        570        580        590        600 
QKFQVYYLGN VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV 

       610        620        630        640        650        660 
LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV QAACMLRYQK 

       670        680        690        700        710 
CLDARSQAST SCLPAPPAES VARRVGWTVR RGVQSLWGSL KPKRLGAHTP 

« Hide

Isoform 2 [UniParc].

Checksum: FC578B7688BCC1A0
Show »

FASTA70876,959
Isoform 3 [UniParc].

Checksum: 72DB1DFEA0886C91
Show »

FASTA48853,927
Isoform 4 (p60Fe65) [UniParc].

Checksum: 14AE683C4BD3A6D5
Show »

FASTA45149,857
Isoform 5 [UniParc].

Checksum: 1996107B7E50C0B0
Show »

FASTA49054,212
Isoform 6 [UniParc].

Checksum: C01AD5CED5941D94
Show »

FASTA47552,656

References

« Hide 'large scale' references
[1]"cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein."
Bressler S.L., Gray M.D., Sopher B.L., Hu Q., Hearn M.G., Pham D.G., Dinulos M.B., Fukuchi K., Sisodia S.S., Miller M.A., Disteche C.M., Martin G.M.
Hum. Mol. Genet. 5:1589-1598(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"The human FE65 gene: genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type."
Hu Q., Kukull W.A., Bressler S.L., Gray M.D., Cam J.A., Larson E.B., Martin G.M., Deeb S.S.
Hum. Genet. 103:295-303(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tissue: Brain.
[3]"Identification and characterization of a neuronal enriched novel transcript encoding the previously described p60Fe65 isoform."
Domingues S.C., Henriques A.G., Fardilha M., da Cruz E Silva E.F., da Cruz E Silva O.A.
J. Neurochem. 119:1086-1098(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Brain.
[4]"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] (ISOFORMS 3; 4 AND 6).
Tissue: Caudate nucleus and Cerebellum.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Fetal brain.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(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 (SEP-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] (ISOFORM 2).
Tissue: Uterus.
[9]"The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to stimulate Fe65/amyloid precursor protein nuclear signaling."
Perkinton M.S., Standen C.L., Lau K.F., Kesavapany S., Byers H.L., Ward M., McLoughlin D.M., Miller C.C.
J. Biol. Chem. 279:22084-22091(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ABL1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-547 BY ABL1, MUTAGENESIS OF TYR-117; TYR-234; TYR-269; TYR-270; TYR-403; TYR-467; 269-TYR--TRP-271; TYR-546 AND TYR-547.
[10]"Human NIMA-related kinase 6 is one of the Fe65 WW domain binding proteins."
Lee E.J., Hyun S.H., Chun J., Kang S.S.
Biochem. Biophys. Res. Commun. 358:783-788(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6.
[11]"Regulation of FE65 nuclear translocation and function by amyloid beta-protein precursor in osmotically stressed cells."
Nakaya T., Kawai T., Suzuki T.
J. Biol. Chem. 283:19119-19131(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH APP.
[12]"Dexras1 interacts with FE65 to regulate FE65-amyloid precursor protein-dependent transcription."
Lau K.-F., Chan W.-M., Perkinton M.S., Tudor E.L., Chang R.C.C., Chan H.-Y., McLoughlin D.M., Miller C.C.J.
J. Biol. Chem. 283:34728-34737(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-547, INTERACTION WITH RASD1, MUTAGENESIS OF TYR-547.
[13]"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions."
Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.
Nature 458:591-596(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH H2AX AND MAPK8.
[14]"FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4."
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.
PLoS ONE 4:E5071-E5071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SET AND TSHZ3, IDENTIFICATION IN A TRIMERIC COMPLEX WITH HDAC1 AND TSHZ3, CHROMATIN-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]"Structural basis for polyproline recognition by the FE65 WW domain."
Meiyappan M., Birrane G., Ladias J.A.A.
J. Mol. Biol. 372:970-980(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 253-289 IN COMPLEX WITH ENAH.
[16]"Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2."
Radzimanowski J., Simon B., Sattler M., Beyreuther K., Sinning I., Wild K.
EMBO Rep. 9:1134-1140(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 534-667 IN COMPLEX WITH APP.
[17]"Crystal structure of the human Fe65-PTB1 domain."
Radzimanowski J., Ravaud S., Schlesinger S., Koch J., Beyreuther K., Sinning I., Wild K.
J. Biol. Chem. 283:23113-23120(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 366-505.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77864 mRNA. Translation: AAB93631.1.
AF029234, AF047835 Genomic DNA. Translation: AAC79942.1.
EF103274 mRNA. Translation: ABL07489.3.
AK293550 mRNA. Translation: BAH11531.1.
AK293554 mRNA. Translation: BAH11532.1.
AK293643 mRNA. Translation: BAH11554.1.
AK295241 mRNA. Translation: BAH12016.1.
BX538185 mRNA. Translation: CAD98057.1. Different initiation.
AC068733 Genomic DNA. No translation available.
AC084337 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68723.1.
CH471064 Genomic DNA. Translation: EAW68724.1.
BC010854 mRNA. Translation: AAH10854.1.
CCDSCCDS31410.1. [O00213-2]
CCDS58114.1. [O00213-3]
CCDS66015.1. [O00213-4]
CCDS66018.1. [O00213-1]
RefSeqNP_001155.1. NM_001164.4. [O00213-1]
NP_001244248.1. NM_001257319.2. [O00213-5]
NP_001244249.1. NM_001257320.2. [O00213-4]
NP_001244250.1. NM_001257321.2. [O00213-4]
NP_001244252.1. NM_001257323.2. [O00213-3]
NP_001244254.1. NM_001257325.2. [O00213-6]
NP_001244255.1. NM_001257326.2. [O00213-4]
NP_663722.1. NM_145689.2. [O00213-2]
UniGeneHs.372840.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E45NMR-A241-290[»]
2HO2X-ray1.33A253-289[»]
2IDHX-ray2.28A/B/C/D/E/F/G/H253-289[»]
2OEIX-ray1.35A253-289[»]
3D8DX-ray2.20A/B366-505[»]
3D8EX-ray2.80A/B/C/D366-505[»]
3D8FX-ray2.70A/B/C/D366-505[»]
3DXCX-ray2.10A/C534-667[»]
3DXDX-ray2.20A/C534-667[»]
3DXEX-ray2.00A/C534-667[»]
ProteinModelPortalO00213.
SMRO00213. Positions 241-290, 366-505, 537-666.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106819. 71 interactions.
DIPDIP-30903N.
IntActO00213. 9 interactions.
MINTMINT-1493266.
STRING9606.ENSP00000299402.

PTM databases

PhosphoSiteO00213.

Proteomic databases

MaxQBO00213.
PaxDbO00213.
PRIDEO00213.

Protocols and materials databases

DNASU322.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299402; ENSP00000299402; ENSG00000166313. [O00213-2]
ENST00000311051; ENSP00000311912; ENSG00000166313. [O00213-2]
ENST00000530885; ENSP00000433338; ENSG00000166313. [O00213-3]
ENST00000608394; ENSP00000476442; ENSG00000166313. [O00213-4]
ENST00000608645; ENSP00000476646; ENSG00000166313. [O00213-4]
ENST00000608655; ENSP00000476846; ENSG00000166313.
ENST00000608704; ENSP00000476871; ENSG00000166313. [O00213-4]
ENST00000609331; ENSP00000477069; ENSG00000166313.
ENST00000609360; ENSP00000477213; ENSG00000166313. [O00213-1]
GeneID322.
KEGGhsa:322.
UCSCuc001mdb.2. human. [O00213-1]
uc001mdc.1. human. [O00213-2]
uc001mdd.4. human.

Organism-specific databases

CTD322.
GeneCardsGC11M006414.
H-InvDBHIX0009398.
HGNCHGNC:581. APBB1.
HPACAB022104.
HPA038521.
HPA038522.
MIM602709. gene.
neXtProtNX_O00213.
PharmGKBPA24873.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG76544.
HOGENOMHOG000033983.
HOVERGENHBG050524.
KOK04529.
OrthoDBEOG79W94P.
PhylomeDBO00213.
TreeFamTF314331.

Enzyme and pathway databases

SignaLinkO00213.

Gene expression databases

ArrayExpressO00213.
BgeeO00213.
CleanExHS_APBB1.
GenevestigatorO00213.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001202. WW_dom.
[Graphical view]
PfamPF00640. PID. 2 hits.
PF00397. WW. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 2 hits.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS01179. PID. 2 hits.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPBB1. human.
EvolutionaryTraceO00213.
GeneWikiAPBB1.
GenomeRNAi322.
NextBio1319.
PROO00213.
SOURCESearch...

Entry information

Entry nameAPBB1_HUMAN
AccessionPrimary (citable) accession number: O00213
Secondary accession number(s): A1E379 expand/collapse secondary AC list , A6NH82, A6NL69, B7Z1J5, B7Z1J6, B7Z2Y0, D3DQT2, Q7Z324, Q96A93, V9GYK0, V9GYT4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 135 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM