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Q92625

- ANS1A_HUMAN

UniProt

Q92625 - ANS1A_HUMAN

Protein

Ankyrin repeat and SAM domain-containing protein 1A

Gene

ANKS1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. ephrin receptor signaling pathway Source: UniProtKB
    2. neuron remodeling Source: UniProtKB
    3. substrate-dependent cell migration Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ankyrin repeat and SAM domain-containing protein 1A
    Alternative name(s):
    Odin
    Gene namesi
    Name:ANKS1A
    Synonyms:ANKS1, KIAA0229, ODIN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20961. ANKS1A.

    Subcellular locationi

    Cytoplasm. Cell projection By similarity
    Note: Cytoplasmic before and after growth factor treatment.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. neuron projection Source: UniProtKB
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cell projection, Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134958476.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 11341133Ankyrin repeat and SAM domain-containing protein 1APRO_0000066921Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Modified residuei318 – 3181Phosphothreonine1 Publication
    Modified residuei622 – 6221Phosphoserine1 Publication
    Modified residuei624 – 6241PhosphoserineBy similarity
    Modified residuei626 – 6261PhosphoserineBy similarity
    Modified residuei647 – 6471Phosphoserine2 Publications
    Modified residuei661 – 6611Phosphoserine3 Publications
    Modified residuei663 – 6631Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated on tyrosine residues in response to EGF and PDGF.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92625.
    PaxDbiQ92625.
    PeptideAtlasiQ92625.
    PRIDEiQ92625.

    PTM databases

    PhosphoSiteiQ92625.

    Expressioni

    Tissue specificityi

    Widely expressed (at protein level).

    Gene expression databases

    ArrayExpressiQ92625.
    BgeeiQ92625.
    CleanExiHS_ANKS1A.
    GenevestigatoriQ92625.

    Organism-specific databases

    HPAiHPA036768.
    HPA036769.

    Interactioni

    Subunit structurei

    Interacts with EPHA8; EPHA8 kinase activity-independent but stimulated by EPHA8 ubiquitination By similarity. Interacts (via SAM domain) with EPHA2 (via SAM domain).By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EGFRP005332EBI-1048612,EBI-297353
    ERBB2P046262EBI-1048612,EBI-641062

    Protein-protein interaction databases

    BioGridi116889. 13 interactions.
    IntActiQ92625. 5 interactions.
    MINTiMINT-1493202.
    STRINGi9606.ENSP00000353518.

    Structurei

    Secondary structure

    1
    1134
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi701 – 7088
    Helixi711 – 7133
    Helixi714 – 7196
    Turni728 – 7303
    Helixi735 – 7417
    Helixi746 – 75712
    Beta strandi759 – 7613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LMRNMR-A691-770[»]
    ProteinModelPortaliQ92625.
    SMRiQ92625. Positions 3-362, 691-832, 933-1063.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati79 – 10830ANK 1Add
    BLAST
    Repeati112 – 14130ANK 2Add
    BLAST
    Repeati148 – 17730ANK 3Add
    BLAST
    Repeati181 – 21030ANK 4Add
    BLAST
    Repeati214 – 24330ANK 5Add
    BLAST
    Repeati246 – 27530ANK 6Add
    BLAST
    Domaini696 – 76267SAM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini770 – 83768SAM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini936 – 1091156PIDPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 5554Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 6 ANK repeats.PROSITE-ProRule annotation
    Contains 1 PID domain.PROSITE-ProRule annotation
    Contains 2 SAM (sterile alpha motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000033973.
    HOVERGENiHBG050506.
    InParanoidiQ92625.
    OMAiTSCHSLD.
    OrthoDBiEOG78H3SN.
    PhylomeDBiQ92625.
    TreeFamiTF320582.

    Family and domain databases

    Gene3Di1.10.150.50. 2 hits.
    1.25.40.20. 4 hits.
    2.30.29.30. 1 hit.
    InterProiIPR002110. 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]
    PfamiPF00023. Ank. 5 hits.
    PF00640. PID. 1 hit.
    PF00536. SAM_1. 2 hits.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 6 hits.
    SM00462. PTB. 1 hit.
    SM00454. SAM. 2 hits.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 2 hits.
    SSF48403. SSF48403. 2 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 6 hits.
    PS01179. PID. 1 hit.
    PS50105. SAM_DOMAIN. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92625-1) [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

    MGKEQELLEA ARTGHLPAVE KLLSGKRLSS GFGGGGGGGS GGGGGGSGGG     50
    GGGLGSSSHP LSSLLSMWRG PNVNCVDSTG YTPLHHAALN GHKDVVEVLL 100
    RNDALTNVAD SKGCYPLHLA AWKGDAQIVR LLIHQGPSHT RVNEQNNDNE 150
    TALHCAAQYG HTEVVKVLLE ELTDPTMRNN KFETPLDLAA LYGRLEVVKM 200
    LLNAHPNLLS CNTKKHTPLH LAARNGHKAV VQVLLDAGMD SNYQTEMGSA 250
    LHEAALFGKT DVVQILLAAG TDVNIKDNHG LTALDTVREL PSQKSQQIAA 300
    LIEDHMTGKR STKEVDKTPP PQPPLISSMD SISQKSQGDV EKAVTELIID 350
    FDANAEEEGP YEALYNAISC HSLDSMASGR SSDQDSTNKE AEAAGVKPAG 400
    VRPRERPPPP AKPPPDEEEE DHIDKKYFPL TASEVLSMRP RIHGSAAREE 450
    DEHPYELLLT AETKKVVLVD GKTKDHRRSS SSRSQDSAEG QDGQVPEQFS 500
    GLLHGSSPVC EVGQDPFQLL CTAGQSHPDG SPQQGACHKA SMQLEETGVH 550
    APGASQPSAL DQSKRVGYLT GLPTTNSRSH PETLTHTASP HPGGAEEGDR 600
    SGARSRAPPT SKPKAELKLS RSLSKSDSDL LTCSPTEDAT MGSRSESLSN 650
    CSIGKKRLEK SPSFASEWDE IEKIMSSIGE GIDFSQERQK ISGLRTLEQS 700
    VGEWLESIGL QQYESKLLLN GFDDVHFLGS NVMEEQDLRD IGISDPQHRR 750
    KLLQAARSLP KVKALGYDGN SPPSVPSWLD SLGLQDYVHS FLSSGYSSID 800
    TVKNLWELEL VNVLKVQLLG HRKRIIASLA DRPYEEPPQK PPRFSQLRCQ 850
    DLLSQTSSPL SQNDSCTGRS ADLLLPPGDT GRRRHDSLHD PAAPSRAERF 900
    RIQEEHREAK LTLRPPSLAA PYAPVQSWQH QPEKLIFESC GYEANYLGSM 950
    LIKDLRGTES TQDACAKMRK STEHMKKIPT IILSITYKGV KFIDASNKNV 1000
    IAEHEIRNIS CAAQDPEDLC TFAYITKDLQ TSHHYCHVFS TVDVNLTYEI 1050
    ILTLGQAFEV AYQLALQAQK SRATGASAAE MIETKSSKPV PKPRVGVRKS 1100
    ALEPPDMDQD AQSHASVSWV VDPKPDSKRS LSTN 1134
    Length:1,134
    Mass (Da):123,108
    Last modified:January 23, 2007 - v4
    Checksum:iE519844AD56EE414
    GO
    Isoform 2 (identifier: Q92625-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         305-320: HMTGKRSTKEVDKTPP → LDTLQFYFISCPFQGL
         321-1134: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:320
    Mass (Da):33,882
    Checksum:i596CAD2B08649EB4
    GO

    Sequence cautioni

    The sequence BAA13218.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti355 – 3551A → D.
    Corresponds to variant rs6930932 [ dbSNP | Ensembl ].
    VAR_048282
    Natural varianti694 – 6941L → S.4 Publications
    Corresponds to variant rs820085 [ dbSNP | Ensembl ].
    VAR_021168

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei305 – 32016HMTGK…DKTPP → LDTLQFYFISCPFQGL in isoform 2. 1 PublicationVSP_056512Add
    BLAST
    Alternative sequencei321 – 1134814Missing in isoform 2. 1 PublicationVSP_056513Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86982 mRNA. Translation: BAA13218.1. Different initiation.
    AK298987 mRNA. Translation: BAG61080.1.
    AL138721, AL033520, AL591002 Genomic DNA. Translation: CAI12437.1.
    AL591002, AL033520, AL138721 Genomic DNA. Translation: CAI15138.1.
    AL033520, AL138721, AL591002 Genomic DNA. Translation: CAI20281.1.
    CH471081 Genomic DNA. Translation: EAX03804.1.
    BC132832 mRNA. Translation: AAI32833.1.
    CCDSiCCDS4798.1.
    RefSeqiNP_056060.2. NM_015245.2.
    UniGeneiHs.656492.

    Genome annotation databases

    EnsembliENST00000360359; ENSP00000353518; ENSG00000064999.
    ENST00000535627; ENSP00000438752; ENSG00000064999.
    GeneIDi23294.
    KEGGihsa:23294.
    UCSCiuc003ojx.4. human.

    Polymorphism databases

    DMDMi62511243.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86982 mRNA. Translation: BAA13218.1 . Different initiation.
    AK298987 mRNA. Translation: BAG61080.1 .
    AL138721 , AL033520 , AL591002 Genomic DNA. Translation: CAI12437.1 .
    AL591002 , AL033520 , AL138721 Genomic DNA. Translation: CAI15138.1 .
    AL033520 , AL138721 , AL591002 Genomic DNA. Translation: CAI20281.1 .
    CH471081 Genomic DNA. Translation: EAX03804.1 .
    BC132832 mRNA. Translation: AAI32833.1 .
    CCDSi CCDS4798.1.
    RefSeqi NP_056060.2. NM_015245.2.
    UniGenei Hs.656492.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LMR NMR - A 691-770 [» ]
    ProteinModelPortali Q92625.
    SMRi Q92625. Positions 3-362, 691-832, 933-1063.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116889. 13 interactions.
    IntActi Q92625. 5 interactions.
    MINTi MINT-1493202.
    STRINGi 9606.ENSP00000353518.

    PTM databases

    PhosphoSitei Q92625.

    Polymorphism databases

    DMDMi 62511243.

    Proteomic databases

    MaxQBi Q92625.
    PaxDbi Q92625.
    PeptideAtlasi Q92625.
    PRIDEi Q92625.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360359 ; ENSP00000353518 ; ENSG00000064999 .
    ENST00000535627 ; ENSP00000438752 ; ENSG00000064999 .
    GeneIDi 23294.
    KEGGi hsa:23294.
    UCSCi uc003ojx.4. human.

    Organism-specific databases

    CTDi 23294.
    GeneCardsi GC06P034857.
    HGNCi HGNC:20961. ANKS1A.
    HPAi HPA036768.
    HPA036769.
    MIMi 608994. gene.
    neXtProti NX_Q92625.
    PharmGKBi PA134958476.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000033973.
    HOVERGENi HBG050506.
    InParanoidi Q92625.
    OMAi TSCHSLD.
    OrthoDBi EOG78H3SN.
    PhylomeDBi Q92625.
    TreeFami TF320582.

    Miscellaneous databases

    ChiTaRSi ANKS1A. human.
    GeneWikii ANKS1A.
    GenomeRNAii 23294.
    NextBioi 45120.
    PROi Q92625.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92625.
    Bgeei Q92625.
    CleanExi HS_ANKS1A.
    Genevestigatori Q92625.

    Family and domain databases

    Gene3Di 1.10.150.50. 2 hits.
    1.25.40.20. 4 hits.
    2.30.29.30. 1 hit.
    InterProi IPR002110. 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 ]
    Pfami PF00023. Ank. 5 hits.
    PF00640. PID. 1 hit.
    PF00536. SAM_1. 2 hits.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 6 hits.
    SM00462. PTB. 1 hit.
    SM00454. SAM. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 2 hits.
    SSF48403. SSF48403. 2 hits.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 6 hits.
    PS01179. PID. 1 hit.
    PS50105. SAM_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-694.
      Tissue: Bone marrow.
    2. "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] (ISOFORM 2).
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-694.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-694.
    6. "Cloning of a novel phosphotyrosine binding domain containing molecule, Odin, involved in signaling by receptor tyrosine kinases."
      Pandey A., Blagoev B., Kratchmarova I., Fernandez M., Nielsen M., Kristiansen T.Z., Ohara O., Podtelejnikov A.V., Roche S., Lodish H.F., Mann M.
      Oncogene 21:8029-8036(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 540-564, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION.
      Tissue: Cervix carcinoma.
    7. "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: FUNCTION IN EFNA5-EPHA8 SIGNALING PATHWAY.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318; SER-622; SER-647 AND SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, VARIANT [LARGE SCALE ANALYSIS] SER-694, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647; SER-661 AND SER-663, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor."
      Mercurio F.A., Marasco D., Pirone L., Pedone E.M., Pellecchia M., Leone M.
      Biochemistry 51:2136-2145(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 691-770, INTERACTION WITH EPHA2.

    Entry informationi

    Entry nameiANS1A_HUMAN
    AccessioniPrimary (citable) accession number: Q92625
    Secondary accession number(s): A2RUC1
    , B4DQW8, Q5JYI9, Q5SYR2, Q86WQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3