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O00213

- APBB1_HUMAN

UniProt

O00213 - APBB1_HUMAN

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Protein

Amyloid beta A4 precursor protein-binding family B member 1

Gene
APBB1, FE65, RIR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).5 Publications

GO - Molecular functioni

  1. beta-amyloid binding Source: UniProtKB
  2. chromatin binding Source: UniProtKB
  3. histone binding Source: UniProtKB
  4. proline-rich region binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. axon guidance Source: Ensembl
  3. axonogenesis Source: UniProtKB
  4. cell cycle arrest Source: UniProtKB
  5. cellular response to DNA damage stimulus Source: UniProtKB
  6. double-strand break repair Source: Ensembl
  7. extracellular matrix organization Source: Ensembl
  8. histone H4 acetylation Source: UniProtKB
  9. negative regulation of cell growth Source: UniProtKB
  10. negative regulation of neuron differentiation Source: Ensembl
  11. negative regulation of thymidylate synthase biosynthetic process Source: UniProtKB
  12. neuron migration Source: Ensembl
  13. positive regulation of apoptotic process Source: UniProtKB
  14. positive regulation of DNA repair Source: Ensembl
  15. positive regulation of transcription, DNA-templated Source: UniProtKB
  16. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  17. regulation of transcription, DNA-templated Source: UniProtKB
  18. signal transduction Source: UniProtKB
  19. transcription, DNA-templated Source: UniProtKB-KW
  20. visual learning Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Repressor

Keywords - Biological processi

Apoptosis, DNA damage, Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiO00213.

Names & Taxonomyi

Protein namesi
Recommended name:
Amyloid beta A4 precursor protein-binding family B member 1
Alternative name(s):
Protein Fe65
Gene namesi
Name:APBB1
Synonyms:FE65, RIR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:581. APBB1.

Subcellular locationi

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.5 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. growth cone Source: UniProtKB
  3. lamellipodium Source: UniProtKB
  4. nuclear speck Source: UniProtKB-SubCell
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: UniProtKB
  7. synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi117 – 1171Y → F: No effect on phosphorylation by ABL1. 1 Publication
Mutagenesisi234 – 2341Y → F: No effect on phosphorylation by ABL1. 1 Publication
Mutagenesisi269 – 2713YYW → AAA: Impairs transcriptional activation and inhibits binding to ABL1. 1 Publication
Mutagenesisi269 – 2691Y → F: No effect on phosphorylation by ABL1. 1 Publication
Mutagenesisi270 – 2701Y → F: No effect on phosphorylation by ABL1. 1 Publication
Mutagenesisi403 – 4031Y → F: No effect on phosphorylation by ABL1. 1 Publication
Mutagenesisi467 – 4671Y → F: No effect on phosphorylation by ABL1. 1 Publication
Mutagenesisi546 – 5461Y → F: No effect on phosphorylation by ABL1. 1 Publication
Mutagenesisi547 – 5471Y → F: Abrogates phosphorylation and stimulation of transcription by ABL1, and increases the interaction with RASD1/DEXRAS1. 2 Publications
Mutagenesisi658 – 6581Y → F: No effect on phosphorylation by ABL1.

Organism-specific databases

PharmGKBiPA24873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 710710Amyloid beta A4 precursor protein-binding family B member 1PRO_0000076049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei547 – 5471Phosphotyrosine; by ABL12 Publications
Modified residuei610 – 6101Phosphoserine; by SGK1 By similarity

Post-translational modificationi

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/DEXRAS1.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00213.
PaxDbiO00213.
PRIDEiO00213.

PTM databases

PhosphoSiteiO00213.

Expressioni

Tissue specificityi

Highly expressed in brain; strongly reduced in post-mortem elderly subjects with Alzheimer disease.1 Publication

Gene expression databases

ArrayExpressiO00213.
BgeeiO00213.
CleanExiHS_APBB1.
GenevestigatoriO00213.

Organism-specific databases

HPAiCAB022104.
HPA038521.
HPA038522.

Interactioni

Subunit structurei

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 ABL1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP050675EBI-81694,EBI-77613
APPP05067-42EBI-81694,EBI-302641
EGFRP005334EBI-81694,EBI-297353
ERBB2P046262EBI-81694,EBI-641062
LRP1Q079543EBI-81694,EBI-1046087

Protein-protein interaction databases

BioGridi106819. 71 interactions.
DIPiDIP-30903N.
IntActiO00213. 9 interactions.
MINTiMINT-1493266.
STRINGi9606.ENSP00000299402.

Structurei

Secondary structure

1
710
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi259 – 2635
Beta strandi268 – 2725
Turni273 – 2753
Beta strandi278 – 2814
Beta strandi368 – 37912
Helixi382 – 3854
Turni387 – 3893
Helixi390 – 40112
Beta strandi421 – 4277
Beta strandi430 – 4345
Turni436 – 4383
Beta strandi441 – 4466
Helixi447 – 4493
Beta strandi452 – 4554
Beta strandi458 – 4603
Beta strandi464 – 4707
Turni472 – 4743
Beta strandi477 – 48610
Helixi488 – 50417
Beta strandi544 – 55411
Helixi559 – 57113
Helixi575 – 5773
Beta strandi579 – 5857
Beta strandi587 – 5948
Turni595 – 5973
Beta strandi600 – 6056
Helixi606 – 6083
Beta strandi609 – 6146
Beta strandi620 – 6289
Beta strandi631 – 64111
Helixi644 – 66522

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO00213.
SMRiO00213. Positions 241-290, 366-505, 537-666.

Miscellaneous databases

EvolutionaryTraceiO00213.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini253 – 28533WWAdd
BLAST
Domaini370 – 509140PID 1Add
BLAST
Domaini542 – 699158PID 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi158 – 17114Glu-richAdd
BLAST

Sequence similaritiesi

Contains 2 PID domains.
Contains 1 WW domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG76544.
HOGENOMiHOG000033983.
HOVERGENiHBG050524.
KOiK04529.
OrthoDBiEOG79W94P.
PhylomeDBiO00213.
TreeFamiTF314331.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00640. PID. 2 hits.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 2 hits.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS01179. PID. 2 hits.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00213-1) [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

MSVPSSLSQS AINANSHGGP ALSLPLPLHA AHNQLLNAKL QATAVGPKDL    50
RSAMGEGGGP EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS 100
QEPEMAPLGP KGLIHLYSEL ELSAHNAANR GLRGPGLIIS TQEQGPDEGE 150
EKAAGEAEEE EEDDDDEEEE EDLSSPPGLP EPLESVEAPP RPQALTDGPR 200
EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT DSFWNPNAFE 250
TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL 300
TWTGFAHGEG FEDGEFWKDE PSDEAPMELG LKEPEEGTLT FPAQSLSPEP 350
LPQEEEKLPP RNTNPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ 400
LSYHKNNLHD PMSGGWGEGK DLLLQLEDET LKLVEPQSQA LLHAQPIISI 450
RVWGVGRDSG RERDFAYVAR DKLTQMLKCH VFRCEAPAKN IATSLHEICS 500
KIMAERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV QKFQVYYLGN 550
VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV 600
LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV 650
QAACMLRYQK CLDARSQAST SCLPAPPAES VARRVGWTVR RGVQSLWGSL 700
KPKRLGAHTP 710
Length:710
Mass (Da):77,244
Last modified:June 1, 1998 - v2
Checksum:iFD4A2EF7E8D8E884
GO
Isoform 2 (identifier: O00213-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     462-463: Missing.

Show »
Length:708
Mass (Da):76,959
Checksum:iFC578B7688BCC1A0
GO
Isoform 3 (identifier: O00213-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:488
Mass (Da):53,927
Checksum:i72DB1DFEA0886C91
GO
Isoform 4 (identifier: O00213-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:451
Mass (Da):49,857
Checksum:i14AE683C4BD3A6D5
GO
Isoform 5 (identifier: O00213-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-213: Missing.
     214-240: NSAASDEDSSWATLSQGSPSYGSPEDT → MSAMFSQDFFLAIILQDSSA

Note: No experimental confirmation available.

Show »
Length:490
Mass (Da):54,212
Checksum:i1996107B7E50C0B0
GO
Isoform 6 (identifier: O00213-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-240: MSVPSSLSQS...SPSYGSPEDT → MTQMR

Note: No experimental confirmation available.

Show »
Length:475
Mass (Da):52,656
Checksum:iC01AD5CED5941D94
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti327 – 3271M → V.
Corresponds to variant rs1800423 [ dbSNP | Ensembl ].
VAR_014444
Natural varianti396 – 3961N → S.
Corresponds to variant rs1800425 [ dbSNP | Ensembl ].
VAR_014445

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 259259Missing in isoform 4. VSP_047459Add
BLAST
Alternative sequencei1 – 240240MSVPS…SPEDT → MTQMR in isoform 6. VSP_054709Add
BLAST
Alternative sequencei1 – 213213Missing in isoform 3 and isoform 5. VSP_045326Add
BLAST
Alternative sequencei214 – 24027NSAAS…SPEDT → MSAMFSQDFFLAIILQDSSA in isoform 3 and isoform 5. VSP_045327Add
BLAST
Alternative sequencei462 – 4632Missing in isoform 2 and isoform 3. VSP_011658

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti367 – 3671I → T in BAH11532. 1 Publication
Sequence conflicti493 – 4931T → A in BAH11532. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31410.1. [O00213-2]
CCDS58114.1. [O00213-3]
CCDS66015.1. [O00213-4]
CCDS66016.1. [O00213-6]
CCDS66017.1. [O00213-5]
CCDS66018.1. [O00213-1]
RefSeqiNP_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]
UniGeneiHs.372840.

Genome annotation databases

EnsembliENST00000299402; 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]
GeneIDi322.
KEGGihsa:322.
UCSCiuc001mdb.2. human. [O00213-1]
uc001mdc.1. human. [O00213-2]
uc001mdd.4. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31410.1. [O00213-2 ]
CCDS58114.1. [O00213-3 ]
CCDS66015.1. [O00213-4 ]
CCDS66016.1. [O00213-6 ]
CCDS66017.1. [O00213-5 ]
CCDS66018.1. [O00213-1 ]
RefSeqi NP_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 ]
UniGenei Hs.372840.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E45 NMR - A 241-290 [» ]
2HO2 X-ray 1.33 A 253-289 [» ]
2IDH X-ray 2.28 A/B/C/D/E/F/G/H 253-289 [» ]
2OEI X-ray 1.35 A 253-289 [» ]
3D8D X-ray 2.20 A/B 366-505 [» ]
3D8E X-ray 2.80 A/B/C/D 366-505 [» ]
3D8F X-ray 2.70 A/B/C/D 366-505 [» ]
3DXC X-ray 2.10 A/C 534-667 [» ]
3DXD X-ray 2.20 A/C 534-667 [» ]
3DXE X-ray 2.00 A/C 534-667 [» ]
ProteinModelPortali O00213.
SMRi O00213. Positions 241-290, 366-505, 537-666.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106819. 71 interactions.
DIPi DIP-30903N.
IntActi O00213. 9 interactions.
MINTi MINT-1493266.
STRINGi 9606.ENSP00000299402.

PTM databases

PhosphoSitei O00213.

Proteomic databases

MaxQBi O00213.
PaxDbi O00213.
PRIDEi O00213.

Protocols and materials databases

DNASUi 322.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000299402 ; 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 ]
GeneIDi 322.
KEGGi hsa:322.
UCSCi uc001mdb.2. human. [O00213-1 ]
uc001mdc.1. human. [O00213-2 ]
uc001mdd.4. human.

Organism-specific databases

CTDi 322.
GeneCardsi GC11M006414.
H-InvDB HIX0009398.
HGNCi HGNC:581. APBB1.
HPAi CAB022104.
HPA038521.
HPA038522.
MIMi 602709. gene.
neXtProti NX_O00213.
PharmGKBi PA24873.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG76544.
HOGENOMi HOG000033983.
HOVERGENi HBG050524.
KOi K04529.
OrthoDBi EOG79W94P.
PhylomeDBi O00213.
TreeFami TF314331.

Enzyme and pathway databases

SignaLinki O00213.

Miscellaneous databases

ChiTaRSi APBB1. human.
EvolutionaryTracei O00213.
GeneWikii APBB1.
GenomeRNAii 322.
NextBioi 1319.
PROi O00213.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00213.
Bgeei O00213.
CleanExi HS_APBB1.
Genevestigatori O00213.

Family and domain databases

Gene3Di 2.30.29.30. 2 hits.
InterProi IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00640. PID. 2 hits.
PF00397. WW. 1 hit.
[Graphical view ]
SMARTi SM00462. PTB. 2 hits.
SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS01179. PID. 2 hits.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Fetal brain.
  6. 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(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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 366-505.

Entry informationi

Entry nameiAPBB1_HUMAN
AccessioniPrimary (citable) accession number: O00213
Secondary accession number(s): A1E379
, A6NH82, A6NL69, B7Z1J5, B7Z1J6, B7Z2Y0, D3DQT2, Q7Z324, Q96A93, V9GYK0, V9GYT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: June 1, 1998
Last modified: September 3, 2014
This is version 136 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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