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Q7Z6G8 (ANS1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1248 AA.
Sequence statusComplete.
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. Ref.2 Ref.8

Isoform 3 can regulate global protein synthesis by altering nucleolar numbers By similarity. Ref.2 Ref.8

Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing. Ref.2 Ref.8

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. Ref.1 Ref.2 Ref.8 Ref.10

Subcellular location

Cytoplasm Ref.1 Ref.2 Ref.8 Ref.11.

Isoform 2: Nucleus Ref.1 Ref.2 Ref.8 Ref.11.

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. Ref.1 Ref.2 Ref.8 Ref.11

Isoform 4: Nucleus. Note: The interaction with APP causes its partial exclusion from the nucleus, when APP is overexpressed. Ref.1 Ref.2 Ref.8 Ref.11

Isoform 6: Nucleus Ref.1 Ref.2 Ref.8 Ref.11.

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. Ref.7 Ref.8

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. Ref.7 Ref.9

Post-translational modification

Isoform 3 nuclear translocation 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.

Sequence caution

The sequence AAP38184.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 10 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:
     1-774: Missing.
     775-807: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     963-1022: Missing.
     1225-1248: DLLHASHTGQEPSERHTEEALRKF → QIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF
Isoform 3 (identifier: Q7Z6G8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-774: Missing.
     775-807: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     1022-1022: Q → QSSVCEIWTNQNAGFPFSAIHQVHN
     1225-1248: DLLHASHTGQEPSERHTEEALRKF → QIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF
Isoform 4 (identifier: Q7Z6G8-4)

Also known as: AIDA-1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-774: Missing.
     775-807: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     1225-1248: DLLHASHTGQEPSERHTEEALRKF → PFCFKADRPI
Isoform 5 (identifier: Q7Z6G8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-774: Missing.
     775-807: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     963-1022: EPSGNHTPPQ...RSKLERQMAQ → SSVCEIWTNQNAGFPFSAIHQVHN
     1225-1248: DLLHASHTGQEPSERHTEEALRKF → QIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF
Isoform 6 (identifier: Q7Z6G8-6)

Also known as: AIDA-1bDeltaAnk;

The sequence of this isoform differs from the canonical sequence as follows:
     1-420: Missing.
     804-807: Missing.
     963-1022: Missing.
Isoform 7 (identifier: Q7Z6G8-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-774: Missing.
     775-807: SFTSEWEEIDKIMSSIDVGINNELKEMNGETTR → MMWQCHLSAQDYRYYPVDGYSLLKRFPLHPLTG
     963-1022: Missing.
Isoform 8 (identifier: Q7Z6G8-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-831: Missing.
     927-1022: VLKINLIGHR...RSKLERQMAQ → QSSVCEIWTNQNAGFPFSAIHQVHN
     1225-1247: DLLHASHTGQEPSERHTEEALRK → IDPSEQKTLANLPWIVEPGQEAKRGINTKYETTI
Isoform 9 (identifier: Q7Z6G8-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-994: Missing.
Note: No experimental confirmation available.
Isoform 10 (identifier: Q7Z6G8-10)

The sequence of this isoform differs from the canonical sequence as follows:
     3-807: Missing.
     963-1022: Missing.
     1225-1247: DLLHASHTGQEPSERHTEEALRK → IDPSEQKTLANLPWIVEPGQEAKRGINTKYETTI
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12481248Ankyrin repeat and sterile alpha motif domain-containing protein 1B
PRO_0000327259

Regions

Repeat2 – 3130ANK 1
Repeat58 – 8730ANK 2
Repeat91 – 12030ANK 3
Repeat127 – 15630ANK 4
Repeat160 – 18930ANK 5
Repeat193 – 22230ANK 6
Repeat225 – 25430ANK 7
Domain810 – 87667SAM 1
Domain884 – 94966SAM 2
Domain1056 – 1213158PID
Motif935 – 9384Nuclear localization signal Ref.11

Amino acid modifications

Modified residue9011Phosphotyrosine By similarity
Modified residue10071Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 994994Missing in isoform 9.
VSP_046414
Alternative sequence1 – 831831Missing in isoform 8.
VSP_032701
Alternative sequence1 – 774774Missing in isoform 3, isoform 4, isoform 5, isoform 2 and isoform 7.
VSP_032702
Alternative sequence1 – 420420Missing in isoform 6.
VSP_032703
Alternative sequence3 – 807805Missing in isoform 10.
VSP_046415
Alternative sequence775 – 80733SFTSE…GETTR → MMWQCHLSAQDYRYYPVDGY SLLKRFPLHPLTG in isoform 3, isoform 4, isoform 5, isoform 2 and isoform 7.
VSP_032704
Alternative sequence804 – 8074Missing in isoform 6.
VSP_032705
Alternative sequence927 – 102296VLKIN…RQMAQ → QSSVCEIWTNQNAGFPFSAI HQVHN in isoform 8.
VSP_032706
Alternative sequence963 – 102260Missing in isoform 2, isoform 6, isoform 7 and isoform 10.
VSP_032707
Alternative sequence963 – 102260EPSGN…RQMAQ → SSVCEIWTNQNAGFPFSAIH QVHN in isoform 5.
VSP_032708
Alternative sequence10221Q → QSSVCEIWTNQNAGFPFSAI HQVHN in isoform 3.
VSP_032709
Alternative sequence1225 – 124824DLLHA…ALRKF → QIDPSEQKTLANLPWIVEPG QEAKRGINTKYETTIF in isoform 3, isoform 5 and isoform 2.
VSP_032710
Alternative sequence1225 – 124824DLLHA…ALRKF → PFCFKADRPI in isoform 4.
VSP_032711
Alternative sequence1225 – 124723DLLHA…EALRK → IDPSEQKTLANLPWIVEPGQ EAKRGINTKYETTI in isoform 8 and isoform 10.
VSP_032712

Experimental info

Sequence conflict290 – 2912RS → KYA in AAP37612. Ref.1
Sequence conflict8131Q → L in BAF82457. Ref.4
Sequence conflict8541E → G in AAI42670. Ref.6
Sequence conflict11601C → R in BAG57507. Ref.4
Sequence conflict11671D → G in BAG58059. Ref.4
Isoform 8:
Sequence conflict3251P → R in AAH68451. Ref.6

Secondary structure

............................................... 1248
Helix Strand Turn

Details...

Sequences

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

Last modified May 3, 2011. Version 2.
Checksum: EC3921C45083426D

FASTA1,248138,066
        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 LQEYLEGVGR STVLEEPVQE 

       310        320        330        340        350        360 
DATQETHISS PVESPSQKTK SETVTGELSK LLDEIKLCQE KDYSFEDLCH TISDHYLDNL 

       370        380        390        400        410        420 
SKISEEELGK NGSQSVRTSS TINLSPGEVE EEDDDENTCG PSGLWEALTP CNGCRNLGFP 

       430        440        450        460        470        480 
MLAQESYPKK RNYTMEIVPS ASLDTFPSEN ENFLCDLMDT AVTKKPCSLE IARAPSPRTD 

       490        500        510        520        530        540 
NASEVAVTTP GTSNHRNSST GPTPDCSPPS PDTALKNIVK VIRPQPKQRT SIVSSLDFHR 

       550        560        570        580        590        600 
MNHNQEYFEI NTSTGCTSFT ASPPASPPTS SVGTTEVKNE GTNHTDDLSR QDDNDPPKEY 

       610        620        630        640        650        660 
DPGQFAGLLH GSSPACESPE NPFHLYGKRE QCEKGQDEVS LANSPLPFKQ SPIENNSEPL 

       670        680        690        700        710        720 
VKKIKPKVVS RTIFHKKSNQ LENHTIVGTR STRSGSRNGD QWVMNAGGFV ERACTLGRIR 

       730        740        750        760        770        780 
SLPKALIDMH LSKSVSKSDS DLIAYPSNEK TSRVNWSESS TAEHSSKGNS ERTPSFTSEW 

       790        800        810        820        830        840 
EEIDKIMSSI DVGINNELKE MNGETTRPRC PVQTVGQWLE SIGLPQYENH LMANGFDNVQ 

       850        860        870        880        890        900 
FMGSNVMEDQ DLLEIGILNS GHRQRILQAI QLLPKMRPIG HDGYHPTSVA EWLDSIELGD 

       910        920        930        940        950        960 
YTKAFLINGY TSMDLLKKIW EVELINVLKI NLIGHRKRIL ASLGDRLHDD PPQKPPRSIT 

       970        980        990       1000       1010       1020 
LREPSGNHTP PQLSPSLSQS TYTTGGSLDV PHIIMQGDAR RRRNENYFDD IPRSKLERQM 

      1030       1040       1050       1060       1070       1080 
AQTGDWGEPS ITLRPPNEAT ASTPVQYWQH HPEKLIFQSC DYKAFYLGSM LIKELRGTES 

      1090       1100       1110       1120       1130       1140 
TQDACAKMRA NCQKSTEQMK KVPTIILSVS YKGVKFIDAT NKNIIAEHEI RNISCAAQDP 

      1150       1160       1170       1180       1190       1200 
EDLSTFAYIT KDLKSNHHYC HVFTAFDVNL AYEIILTLGQ AFEVAYQLAL QARKGGHSST 

      1210       1220       1230       1240 
LPESFENKPS KPIPKPRVSI RKSVDLLHAS HTGQEPSERH TEEALRKF 

« Hide

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

Checksum: 0AE12663DD16CAC2
Show »

FASTA42648,432
Isoform 3 [UniParc].

Checksum: 882DB0117D894E54
Show »

FASTA51057,865
Isoform 4 (AIDA-1a) [UniParc].

Checksum: 34A6DD31C86685CD
Show »

FASTA46052,273
Isoform 5 [UniParc].

Checksum: 7513E87841E4A57C
Show »

FASTA45051,100
Isoform 6 (AIDA-1bDeltaAnk) [UniParc].

Checksum: 7C107E6688522EF0
Show »

FASTA76485,202
Isoform 7 [UniParc].

Checksum: AD92EB5F8954E011
Show »

FASTA41447,104
Isoform 8 [UniParc].

Checksum: 07892A522BFC2835
Show »

FASTA35740,277
Isoform 9 [UniParc].

Checksum: 33299F04446DCF7F
Show »

FASTA25428,943
Isoform 10 [UniParc].

Checksum: D921575BBFF3C4C6
Show »

FASTA39444,522

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 9 AND 10).
Tissue: Amygdala and Brain.
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 3; 5; 7 AND 8).
Tissue: Brain and Hippocampus.
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 294-1248 (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY.
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-1192 (ISOFORM 1), FUNCTION, INTERACTION WITH APP, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"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] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHA8.
[11]"A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import."
Kurabi A., Brener S., Mobli M., Kwan J.J., Donaldson L.W.
J. Mol. Biol. 392:1168-1177(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 813-947, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY281131 mRNA. Translation: AAP37612.1.
AY281132 mRNA. Translation: AAP37613.1.
AY283057 mRNA. Translation: AAP38184.2. Different initiation.
AY753193 mRNA. Translation: AAV28691.1.
AF164792 mRNA. Translation: AAF80756.1.
AK289768 mRNA. Translation: BAF82457.1.
AK294191 mRNA. Translation: BAG57507.1.
AK294994 mRNA. Translation: BAG58059.1.
AC008126 Genomic DNA. No translation available.
AC011248 Genomic DNA. No translation available.
AC021653 Genomic DNA. No translation available.
AC048330 Genomic DNA. No translation available.
AC069437 Genomic DNA. No translation available.
AC078916 Genomic DNA. No translation available.
AC079954 Genomic DNA. No translation available.
AC084374 Genomic DNA. No translation available.
AC117377 Genomic DNA. No translation available.
AC126616 Genomic DNA. No translation available.
AC141554 Genomic DNA. No translation available.
AC141555 Genomic DNA. No translation available.
AC141556 Genomic DNA. No translation available.
BC026313 mRNA. Translation: AAH26313.2.
BC068451 mRNA. Translation: AAH68451.1.
BC142669 mRNA. Translation: AAI42670.1.
BC150204 mRNA. Translation: AAI50205.1.
AF145204 mRNA. Translation: AAD33951.1.
AY620824 mRNA. Translation: AAT39519.1.
CCDSCCDS55864.1. [Q7Z6G8-9]
CCDS55865.1. [Q7Z6G8-8]
CCDS55866.1. [Q7Z6G8-7]
CCDS55867.1. [Q7Z6G8-2]
CCDS55868.1. [Q7Z6G8-5]
CCDS55869.1. [Q7Z6G8-4]
CCDS55870.1. [Q7Z6G8-3]
CCDS55871.1. [Q7Z6G8-10]
CCDS55872.1. [Q7Z6G8-1]
RefSeqNP_001190994.1. NM_001204065.1.
NP_001190995.1. NM_001204066.1. [Q7Z6G8-8]
NP_001190996.1. NM_001204067.1. [Q7Z6G8-10]
NP_001190997.1. NM_001204068.1. [Q7Z6G8-4]
NP_001190998.1. NM_001204069.1. [Q7Z6G8-5]
NP_001190999.1. NM_001204070.1. [Q7Z6G8-2]
NP_001191008.1. NM_001204079.1.
NP_001191009.1. NM_001204080.1.
NP_001191010.1. NM_001204081.1. [Q7Z6G8-9]
NP_064525.1. NM_020140.3. [Q7Z6G8-7]
NP_690001.3. NM_152788.4. [Q7Z6G8-1]
NP_858056.2. NM_181670.3. [Q7Z6G8-3]
UniGeneHs.506458.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EAMNMR-A808-874[»]
2KE7NMR-A808-893[»]
2KIVNMR-A812-946[»]
2M38NMR-A1042-1194[»]
ProteinModelPortalQ7Z6G8.
SMRQ7Z6G8. Positions 5-307, 812-946, 1053-1187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121229. 7 interactions.
IntActQ7Z6G8. 3 interactions.
MINTMINT-258807.

PTM databases

PhosphoSiteQ7Z6G8.

Polymorphism databases

DMDM332278155.

Proteomic databases

PaxDbQ7Z6G8.
PRIDEQ7Z6G8.

Protocols and materials databases

DNASU56899.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341752; ENSP00000345510; ENSG00000185046. [Q7Z6G8-9]
ENST00000546568; ENSP00000448205; ENSG00000185046. [Q7Z6G8-2]
ENST00000546960; ENSP00000447839; ENSG00000185046. [Q7Z6G8-4]
ENST00000547010; ENSP00000448512; ENSG00000185046. [Q7Z6G8-6]
ENST00000547446; ENSP00000450015; ENSG00000185046. [Q7Z6G8-10]
ENST00000547776; ENSP00000449629; ENSG00000185046. [Q7Z6G8-1]
ENST00000549025; ENSP00000447312; ENSG00000185046. [Q7Z6G8-8]
ENST00000549493; ENSP00000448203; ENSG00000185046. [Q7Z6G8-3]
ENST00000549558; ENSP00000448993; ENSG00000185046. [Q7Z6G8-7]
ENST00000550693; ENSP00000447999; ENSG00000185046. [Q7Z6G8-5]
GeneID56899.
KEGGhsa:56899.
UCSCuc001tgd.2. human. [Q7Z6G8-7]
uc001tge.2. human. [Q7Z6G8-1]
uc001tgf.2. human. [Q7Z6G8-6]
uc001tgi.3. human. [Q7Z6G8-3]
uc001tgj.3. human. [Q7Z6G8-2]
uc009ztr.3. human. [Q7Z6G8-5]
uc009zts.2. human. [Q7Z6G8-4]

Organism-specific databases

CTD56899.
GeneCardsGC12M099129.
HGNCHGNC:24600. ANKS1B.
HPAHPA044628.
MIM607815. gene.
neXtProtNX_Q7Z6G8.
PharmGKBPA128394692.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG050506.
InParanoidQ7Z6G8.
OMARNGDQWV.
OrthoDBEOG78H3SN.
TreeFamTF320582.

Gene expression databases

ArrayExpressQ7Z6G8.
BgeeQ7Z6G8.
GenevestigatorQ7Z6G8.

Family and domain databases

Gene3D1.10.150.50. 2 hits.
1.25.40.20. 3 hits.
2.30.29.30. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
[Graphical view]
PfamPF12796. Ank_2. 2 hits.
PF00640. PID. 1 hit.
PF00536. SAM_1. 2 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 6 hits.
SM00462. PTB. 1 hit.
SM00454. SAM. 2 hits.
[Graphical view]
SUPFAMSSF47769. SSF47769. 2 hits.
SSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01179. PID. 1 hit.
PS50105. SAM_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANKS1B. human.
EvolutionaryTraceQ7Z6G8.
GeneWikiANKS1B.
GenomeRNAi56899.
NextBio62343.
PROQ7Z6G8.
SOURCESearch...

Entry information

Entry nameANS1B_HUMAN
AccessionPrimary (citable) accession number: Q7Z6G8
Secondary accession number(s): A5PKY5 expand/collapse secondary AC list , A7E259, A8K153, A8MSN4, B4DFP6, B4DH98, F8VPM3, F8VZR9, F8WC27, Q5XLJ0, Q6IVB5, Q6NUS4, Q7Z6G6, Q7Z6G7, Q8TAP3, Q9NRX7, Q9Y5K9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 3, 2011
Last modified: July 9, 2014
This is version 96 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 chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM