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Reviewed, UniProtKB/Swiss-Prot Q7Z6G8 (ANS1B_HUMAN)

Last modified September 2, 2008. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ankyrin repeat and sterile alpha motif domain-containing protein 1B
Alternative name(s):
    Amyloid-beta protein intracellular domain-associated protein 1
      Short name=AIDA-1
    E2A-PBX1-associated protein
      Short name=EB-1
Gene names
Name: ANKS1B
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.

Isoform 3 can regulate global protein synthesis by altering nucleolar numbers By similarity.

Isoform 4 may play a role as a modulator of APP processing. Overexpression of isoform 4 can down-regulate APP processing.

Subunit structure

Isoform 3 interacts with DLG4 By similarity. Interacts with EPHA8. Isoform 2 interacts with COIL. Isoform 4 interacts with APP and EPHA8. Isoform 6 interacts with EPHA8.

Subcellular location

Cytoplasm.

Isoform 2: Nucleus.

Isoform 3: Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell projectiondendritic spine. Nucleus. NucleusCajal body. Note= The synaptic localization requires DLG4 interaction. Translocation to the nucleus in response to stimulation of NMDA receptors (NMDARs) in a calcium-independent manner By similarity.

Isoform 4: Nucleus. Note= The interaction with APP causes its partial exclusion from the nucleus, when APP is overexpressed.

Isoform 6: Nucleus.

Tissue specificity

Highly expressed in marrow from patients with pre-B ALL associated with the t(1;19) translocation. Strongly expressed in brain and testis. Expressed in fetal brain. Isoform 4 is highly expressed in brain (at protein level). Isoform 6 is expressed in brain and several cancer cell lines.

Induction

Transcriptionally up-regulated in t(1:19) pre-B cell acute lymphocytic leukemia by the chimeric TCF3-PBX1. Not expressed in pre-B cell that lack this translocation.

Post-translational modification

Nuclear translocation of isoform 3 requires an NMDAR-dependent proteolytic cleavage By similarity.

Sequence similarities

Contains 7 ANK repeats.

Contains 1 PID domain.

Contains 2 SAM (sterile alpha motif) domains.

Ontologies

Keywords

   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Nucleus
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Repeat
   PTMPhosphoprotein

Gene Ontology (GO)

None. [Check GOA]

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z6G8-1)

Also known as: AIDA-1b;

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: Q7Z6G8-2)

Also known as: AIDA-1c;

The sequence of this isoform differs from the canonical sequence as follows:
     1-775: Missing.
     776-808: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     964-1023: Missing.
     1226-1249: DLLHASHTGQEPSERHTEEALRKF → QIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF
Isoform 3 (identifier: Q7Z6G8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-775: Missing.
     776-808: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     1023-1023: Q → QSSVCEIWTNQNAGFPFSAIHQVHN
     1226-1249: DLLHASHTGQEPSERHTEEALRKF → QIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF
Notes: The synaptic localization requires DLG4 interaction. Translocation to the nucleus in response to stimulation of NMDA receptors (NMDARs) in a calcium-independent manner (By similarity).
Isoform 4 (identifier: Q7Z6G8-4)

Also known as: AIDA-1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-775: Missing.
     776-808: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     1226-1249: DLLHASHTGQEPSERHTEEALRKF → PFCFKADRPI
Notes: The interaction with APP causes its partial exclusion from the nucleus, when APP is overexpressed.
Isoform 5 (identifier: Q7Z6G8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-775: Missing.
     776-808: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     964-1023: EPSGNHTPPQ...RSKLERQMAQ → SSVCEIWTNQNAGFPFSAIHQVHN
     1226-1249: DLLHASHTGQEPSERHTEEALRKF → QIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF
Isoform 6 (identifier: Q7Z6G8-6)

Also known as: AIDA-1bDeltaAnk;

The sequence of this isoform differs from the canonical sequence as follows:
     1-421: Missing.
     805-808: Missing.
     964-1023: Missing.
Isoform 7 (identifier: Q7Z6G8-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-775: Missing.
     776-808: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     964-1023: Missing.
Isoform 8 (identifier: Q7Z6G8-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-832: Missing.
     928-1023: VLKINLIGHR...RSKLERQMAQ → QSSVCEIWTNQNAGFPFSAIHQVHN
     1226-1249: DLLHASHTGQEPSERHTEEALRKF → IDRSEQKTLANLPWIVEPGQEAKRGINTKYETTIF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 12491248Ankyrin repeat and sterile alpha motif domain-containing protein 1B

Regions

Repeat2 – 3130ANK 1
Repeat58 – 8730ANK 2
Repeat91 – 12030ANK 3
Repeat127 – 15630ANK 4
Repeat160 – 18930ANK 5
Repeat193 – 22230ANK 6
Repeat225 – 25430ANK 7
Domain811 – 87767SAM 1
Domain885 – 95066SAM 2
Domain1057 – 1214158PID

Amino acid modifications

Modified residue9021Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 832832Missing in isoform 8.
Alternative sequence1 – 775775Missing in isoform 3, isoform 4, isoform 5, isoform 2 and isoform 7.
Alternative sequence1 – 421421Missing in isoform 6.
Alternative sequence776 – 80833SFTSE…GETTR → MMWQCHLSAQDYRYYPVDGY SLLKRFPLHPLTG in isoform 3, isoform 4, isoform 5, isoform 2 and isoform 7.
Alternative sequence805 – 8084Missing in isoform 6.
Alternative sequence928 – 102396VLKIN…RQMAQ → QSSVCEIWTNQNAGFPFSAI HQVHN in isoform 8.
Alternative sequence964 – 102360Missing in isoform 2, isoform 6 and isoform 7.
Alternative sequence964 – 102360EPSGN…RQMAQ → SSVCEIWTNQNAGFPFSAIH QVHN in isoform 5.
Alternative sequence10231Q → QSSVCEIWTNQNAGFPFSAI HQVHN in isoform 3.
Alternative sequence1226 – 124924DLLHA…ALRKF → QIDPSEQKTLANLPWIVEPG QEAKRGINTKYETTIF in isoform 3, isoform 5 and isoform 2.
Alternative sequence1226 – 124924DLLHA…ALRKF → PFCFKADRPI in isoform 4.
Alternative sequence1226 – 124924DLLHA…ALRKF → IDRSEQKTLANLPWIVEPGQ EAKRGINTKYETTIF in isoform 8.

Experimental info

Sequence conflict8141Q → L in BAF82457. Ref.4
Sequence conflict8551E → G in AAI42670. Ref.5

Sequences

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

Last modified October 1, 2003. Version 1.
Checksum: B8CDF79E1EF027A7

FASTA1,249138,185
        10         20         30         40         50         60 
MGKDQELLEA ARTGNVALVE KLLSGRKGGI LGGGSGPLPL SNLLSIWRGP NVNCTDSSGY 

        70         80         90        100        110        120 
TALHHAALNG HKDIVLKLLQ YEASTNVADN KGYFPIHLAA WKGDVEIVKI LIHHGPSHSR 

       130        140        150        160        170        180 
VNEQNNENET ALHCAAQYGH SEVVAVLLEE LTDPTIRNSK LETPLDLAAL YGRLRVVKMI 

       190        200        210        220        230        240 
ISAHPNLMSC NTRKHTPLHL AARNGHKAVV QVLLEAGMDV SCQTEKGSAL HEAALFGKVD 

       250        260        270        280        290        300 
VVRVLLETGI DANIKDSLGR TVLDILKEHP SQKSLQIATL LQEYLEGVGK YATVLEEPVQ 

       310        320        330        340        350        360 
EDATQETHIS SPVESPSQKT KSETVTGELS KLLDEIKLCQ EKDYSFEDLC HTISDHYLDN 

       370        380        390        400        410        420 
LSKISEEELG KNGSQSVRTS STINLSPGEV EEEDDDENTC GPSGLWEALT PCNGCRNLGF 

       430        440        450        460        470        480 
PMLAQESYPK KRNYTMEIVP SASLDTFPSE NENFLCDLMD TAVTKKPCSL EIARAPSPRT 

       490        500        510        520        530        540 
DNASEVAVTT PGTSNHRNSS TGPTPDCSPP SPDTALKNIV KVIRPQPKQR TSIVSSLDFH 

       550        560        570        580        590        600 
RMNHNQEYFE INTSTGCTSF TASPPASPPT SSVGTTEVKN EGTNHTDDLS RQDDNDPPKE 

       610        620        630        640        650        660 
YDPGQFAGLL HGSSPACESP ENPFHLYGKR EQCEKGQDEV SLANSPLPFK QSPIENNSEP 

       670        680        690        700        710        720 
LVKKIKPKVV SRTIFHKKSN QLENHTIVGT RSTRSGSRNG DQWVMNAGGF VERACTLGRI 

       730        740        750        760        770        780 
RSLPKALIDM HLSKSVSKSD SDLIAYPSNE KTSRVNWSES STAEHSSKGN SERTPSFTSE 

       790        800        810        820        830        840 
WEEIDKIMSS IDVGINNELK EMNGETTRPR CPVQTVGQWL ESIGLPQYEN HLMANGFDNV 

       850        860        870        880        890        900 
QFMGSNVMED QDLLEIGILN SGHRQRILQA IQLLPKMRPI GHDGYHPTSV AEWLDSIELG 

       910        920        930        940        950        960 
DYTKAFLING YTSMDLLKKI WEVELINVLK INLIGHRKRI LASLGDRLHD DPPQKPPRSI 

       970        980        990       1000       1010       1020 
TLREPSGNHT PPQLSPSLSQ STYTTGGSLD VPHIIMQGDA RRRRNENYFD DIPRSKLERQ 

      1030       1040       1050       1060       1070       1080 
MAQTGDWGEP SITLRPPNEA TASTPVQYWQ HHPEKLIFQS CDYKAFYLGS MLIKELRGTE 

      1090       1100       1110       1120       1130       1140 
STQDACAKMR ANCQKSTEQM KKVPTIILSV SYKGVKFIDA TNKNIIAEHE IRNISCAAQD 

      1150       1160       1170       1180       1190       1200 
PEDLSTFAYI TKDLKSNHHY CHVFTAFDVN LAYEIILTLG QAFEVAYQLA LQARKGGHSS 

      1210       1220       1230       1240 
TLPESFENKP SKPIPKPRVS IRKSVDLLHA SHTGQEPSER HTEEALRKF 

« Hide

Isoform 2 (AIDA-1c) [UniParc].

Checksum: 0AE12663DD16CAC2
Show »

42648,432
Isoform 3 [UniParc].

Checksum: 882DB0117D894E54
Show »

51057,865
Isoform 4 (AIDA-1a) [UniParc].

Checksum: 34A6DD31C86685CD
Show »

46052,273
Isoform 5 [UniParc].

Checksum: 7513E87841E4A57C
Show »

45051,100
Isoform 6 (AIDA-1bDeltaAnk) [UniParc].

Checksum: 7C107E6688522EF0
Show »

76485,202
Isoform 7 [UniParc].

Checksum: AD92EB5F8954E011
Show »

41447,104
Isoform 8 [UniParc].

Checksum: 04DF1F322BFC2835
Show »

35740,336

References

« Hide 'large scale' references
[1]"The intracellular localization of amyloid beta protein precursor (AbetaPP) intracellular domain associated protein-1 (AIDA-1) is regulated by AbetaPP and alternative splicing."
Ghersi E., Vito P., Lopez P., Abdallah M., D'Adamio L.
J. Alzheimers Dis. 6:67-78(2004) [PubMed: 15004329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 4), INTERACTION WITH APP, SUBCELLULAR LOCATION.
Tissue: Fetal brain.
[2]"A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin."
Xu H., Hebert M.D.
BMC Cell Biol. 6:23-23(2005) [PubMed: 15862129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH COIL, SUBCELLULAR LOCATION.
Tissue: Brain.
[3]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Adrenal gland.
[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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5; 7 AND 8).
Tissue: Brain and Hippocampus.
[6]"EB-1, a tyrosine kinase signal transduction gene, is transcriptionally activated in the t(1;19) subset of pre-B ALL, which express oncoprotein E2a-Pbx1."
Fu X., McGrath S., Pasillas M., Nakazawa S., Kamps M.P.
Oncogene 18:4920-4929(1999) [PubMed: 10490826] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 294-1248 (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY.
[7]"Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner."
Ghersi E., Noviello C., D'Adamio L.
J. Biol. Chem. 279:49105-49112(2004) [PubMed: 15347684] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-1192 (ISOFORM 1), FUNCTION, INTERACTION WITH APP, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"The effects of siRNA-mediated inhibition of E2A-PBX1 on EB-1 and Wnt16b expression in the 697 pre-B leukemia cell line."
Casagrande G., te Kronnie G., Basso G.
Haematologica 91:765-771(2006) [PubMed: 16769578] [Abstract]
Cited for: INDUCTION.
[9]"Identification of phosphotyrosine binding domain-containing proteins as novel downstream targets of the EphA8 signaling function."
Shin J., Gu C., Park E., Park S.
Mol. Cell. Biol. 27:8113-8126(2007) [PubMed: 17875921] [Abstract]
Cited for: INTERACTION WITH EPHA8.
+Additional computationally mapped references.

Cross-references