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Q9UEY8

- ADDG_HUMAN

UniProt

Q9UEY8 - ADDG_HUMAN

Protein

Gamma-adducin

Gene

ADD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin.

    GO - Molecular functioni

    1. structural constituent of cytoskeleton Source: ProtInc

    Keywords - Ligandi

    Actin-binding, Calmodulin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-adducin
    Alternative name(s):
    Adducin-like protein 70
    Gene namesi
    Name:ADD3
    Synonyms:ADDL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:245. ADD3.

    Subcellular locationi

    GO - Cellular componenti

    1. cell-cell junction Source: Ensembl
    2. cell cortex Source: Ensembl
    3. condensed nuclear chromosome Source: Ensembl
    4. cytoskeleton Source: UniProtKB-SubCell
    5. membrane Source: ProtInc
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti210141. Inherited congenital spastic tetraplegia.
    PharmGKBiPA24567.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 706705Gamma-adducinPRO_0000218536Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei42 – 421Phosphoserine2 Publications
    Modified residuei64 – 641Phosphoserine1 Publication
    Modified residuei402 – 4021Phosphoserine1 Publication
    Modified residuei423 – 4231Phosphoserine2 Publications
    Modified residuei442 – 4421Phosphoserine1 Publication
    Modified residuei673 – 6731Phosphoserine3 Publications
    Modified residuei677 – 6771Phosphoserine3 Publications
    Modified residuei681 – 6811Phosphoserine3 Publications
    Modified residuei683 – 6831Phosphoserine; by PKCBy similarity

    Post-translational modificationi

    Sumoylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UEY8.
    PaxDbiQ9UEY8.
    PRIDEiQ9UEY8.

    PTM databases

    PhosphoSiteiQ9UEY8.

    Miscellaneous databases

    PMAP-CutDBQ9UEY8.

    Expressioni

    Tissue specificityi

    Isoform 1 is ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9UEY8.
    BgeeiQ9UEY8.
    CleanExiHS_ADD3.
    GenevestigatoriQ9UEY8.

    Organism-specific databases

    HPAiCAB009797.
    HPA035696.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a gamma subunit.

    Protein-protein interaction databases

    BioGridi106633. 5 interactions.
    IntActiQ9UEY8. 5 interactions.
    STRINGi9606.ENSP00000348381.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UEY8.
    SMRiQ9UEY8. Positions 153-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni684 – 70118Interaction with calmodulinSequence AnalysisAdd
    BLAST

    Domaini

    Comprised of three regions: a N-terminal protease-resistant globular head region, a short connecting subdomain, and a protease-sensitive tail region.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0235.
    HOGENOMiHOG000116349.
    HOVERGENiHBG004180.
    InParanoidiQ9UEY8.
    OMAiVNVPEES.
    OrthoDBiEOG7HF1HR.
    PhylomeDBiQ9UEY8.
    TreeFamiTF313003.

    Family and domain databases

    Gene3Di3.40.225.10. 1 hit.
    InterProiIPR027772. ADD3.
    IPR001303. Aldolase_II/adducin_N.
    [Graphical view]
    PANTHERiPTHR10672:SF5. PTHR10672:SF5. 1 hit.
    PfamiPF00596. Aldolase_II. 1 hit.
    [Graphical view]
    SMARTiSM01007. Aldolase_II. 1 hit.
    [Graphical view]
    SUPFAMiSSF53639. SSF53639. 1 hit.

    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

    Note: Additional isoforms seem to exist.

    Isoform 2 (identifier: Q9UEY8-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MSSDASQGVI TTPPPPSMPH KERYFDRINE NDPEYIRERN MSPDLRQDFN    50
    MMEQRKRVTQ ILQSPAFRED LECLIQEQMK KGHNPTGLLA LQQIADYIMA 100
    NSFSGFSSPP LSLGMVTPIN DLPGADTSSY VKGEKLTRCK LASLYRLVDL 150
    FGWAHLANTY ISVRISKEQD HIIIIPRGLS FSEATASNLV KVNIIGEVVD 200
    QGSTNLKIDH TGFSPHAAIY STRPDVKCVI HIHTLATAAV SSMKCGILPI 250
    SQESLLLGDV AYYDYQGSLE EQEERIQLQK VLGPSCKVLV LRNHGVVALG 300
    ETLEEAFHYI FNVQLACEIQ VQALAGAGGV DNLHVLDFQK YKAFTYTVAA 350
    SGGGGVNMGS HQKWKVGEIE FEGLMRTLDN LGYRTGYAYR HPLIREKPRH 400
    KSDVEIPATV TAFSFEDDTV PLSPLKYMAQ RQQREKTRWL NSPNTYMKVN 450
    VPEESRNGET SPRTKITWMK AEDSSKVSGG TPIKIEDPNQ FVPLNTNPNE 500
    VLEKRNKIRE QNRYDLKTAG PQSQLLAGIV VDKPPSTMQF EDDDHGPPAP 550
    PNPFSHLTEG ELEEYKRTIE RKQQGLEDAE QELLSDDASS VSQIQSQTQS 600
    PQNVPEKLEE NHELFSKSFI SMEVPVMVVN GKDDMHDVED ELAKRVSRLS 650
    TSTTIENIEI TIKSPEKIEE VLSPEGSPSK SPSKKKKKFR TPSFLKKNKK 700
    KEKVEA 706
    Length:706
    Mass (Da):79,155
    Last modified:May 1, 2000 - v1
    Checksum:iEB8EAF602A4D7B41
    GO
    Isoform 1 (identifier: Q9UEY8-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         576-607: Missing.

    Show »
    Length:674
    Mass (Da):75,671
    Checksum:i28935F90F7C17BD9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 502FN → SS in BAA23783. (PubMed:8893809)Curated
    Sequence conflicti60 – 601Q → R in BAA23783. (PubMed:8893809)Curated
    Sequence conflicti362 – 3621Q → P in AAB17126. 1 PublicationCurated
    Sequence conflicti420 – 4201V → M in AAB17126. 1 PublicationCurated
    Sequence conflicti421 – 4211P → L in BAA23783. (PubMed:8893809)Curated
    Sequence conflicti426 – 4338KYMAQRQQ → QIHGTRGNK in AAB17126. 1 PublicationCurated
    Sequence conflicti484 – 4841K → Q in AAB17126. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei576 – 60732Missing in isoform 1. 3 PublicationsVSP_000188Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D67031 mRNA. Translation: BAA23783.1.
    U37122 mRNA. Translation: AAB17126.1.
    Y14372
    , Y14373, Y14374, Y14375, Y14376, Y14377, Y14378, Y14379, Y14380, Y14381, Y14382, Y14383, Y14384 Genomic DNA. Translation: CAB51805.1.
    Y14372
    , Y14373, Y14374, Y14375, Y14376, Y14377, Y14378, Y14379, Y14380, Y14381, Y14382, Y14384 Genomic DNA. Translation: CAB51806.1.
    BX647403 mRNA. Translation: CAI46048.1.
    AL590628 Genomic DNA. Translation: CAH71739.1.
    CH471066 Genomic DNA. Translation: EAW49573.1.
    CH471066 Genomic DNA. Translation: EAW49574.1.
    BC062559 mRNA. Translation: AAH62559.1.
    CCDSiCCDS7561.1. [Q9UEY8-1]
    CCDS7562.1. [Q9UEY8-2]
    PIRiJC7164.
    RefSeqiNP_001112.2. NM_001121.2. [Q9UEY8-2]
    NP_058432.1. NM_016824.3. [Q9UEY8-1]
    NP_063968.1. NM_019903.3. [Q9UEY8-2]
    XP_005269586.1. XM_005269529.1. [Q9UEY8-1]
    XP_005269587.1. XM_005269530.1. [Q9UEY8-1]
    XP_005269588.1. XM_005269531.2. [Q9UEY8-1]
    XP_005269590.1. XM_005269533.1. [Q9UEY8-1]
    XP_005269591.1. XM_005269534.2. [Q9UEY8-1]
    XP_006717689.1. XM_006717626.1. [Q9UEY8-1]
    XP_006717690.1. XM_006717627.1. [Q9UEY8-1]
    XP_006717691.1. XM_006717628.1. [Q9UEY8-1]
    UniGeneiHs.501012.

    Genome annotation databases

    EnsembliENST00000277900; ENSP00000277900; ENSG00000148700. [Q9UEY8-2]
    ENST00000356080; ENSP00000348381; ENSG00000148700. [Q9UEY8-1]
    ENST00000360162; ENSP00000353286; ENSG00000148700. [Q9UEY8-2]
    GeneIDi120.
    KEGGihsa:120.
    UCSCiuc001kys.4. human. [Q9UEY8-2]
    uc001kyt.4. human. [Q9UEY8-1]

    Polymorphism databases

    DMDMi12643881.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D67031 mRNA. Translation: BAA23783.1 .
    U37122 mRNA. Translation: AAB17126.1 .
    Y14372
    , Y14373 , Y14374 , Y14375 , Y14376 , Y14377 , Y14378 , Y14379 , Y14380 , Y14381 , Y14382 , Y14383 , Y14384 Genomic DNA. Translation: CAB51805.1 .
    Y14372
    , Y14373 , Y14374 , Y14375 , Y14376 , Y14377 , Y14378 , Y14379 , Y14380 , Y14381 , Y14382 , Y14384 Genomic DNA. Translation: CAB51806.1 .
    BX647403 mRNA. Translation: CAI46048.1 .
    AL590628 Genomic DNA. Translation: CAH71739.1 .
    CH471066 Genomic DNA. Translation: EAW49573.1 .
    CH471066 Genomic DNA. Translation: EAW49574.1 .
    BC062559 mRNA. Translation: AAH62559.1 .
    CCDSi CCDS7561.1. [Q9UEY8-1 ]
    CCDS7562.1. [Q9UEY8-2 ]
    PIRi JC7164.
    RefSeqi NP_001112.2. NM_001121.2. [Q9UEY8-2 ]
    NP_058432.1. NM_016824.3. [Q9UEY8-1 ]
    NP_063968.1. NM_019903.3. [Q9UEY8-2 ]
    XP_005269586.1. XM_005269529.1. [Q9UEY8-1 ]
    XP_005269587.1. XM_005269530.1. [Q9UEY8-1 ]
    XP_005269588.1. XM_005269531.2. [Q9UEY8-1 ]
    XP_005269590.1. XM_005269533.1. [Q9UEY8-1 ]
    XP_005269591.1. XM_005269534.2. [Q9UEY8-1 ]
    XP_006717689.1. XM_006717626.1. [Q9UEY8-1 ]
    XP_006717690.1. XM_006717627.1. [Q9UEY8-1 ]
    XP_006717691.1. XM_006717628.1. [Q9UEY8-1 ]
    UniGenei Hs.501012.

    3D structure databases

    ProteinModelPortali Q9UEY8.
    SMRi Q9UEY8. Positions 153-373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106633. 5 interactions.
    IntActi Q9UEY8. 5 interactions.
    STRINGi 9606.ENSP00000348381.

    PTM databases

    PhosphoSitei Q9UEY8.

    Polymorphism databases

    DMDMi 12643881.

    Proteomic databases

    MaxQBi Q9UEY8.
    PaxDbi Q9UEY8.
    PRIDEi Q9UEY8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000277900 ; ENSP00000277900 ; ENSG00000148700 . [Q9UEY8-2 ]
    ENST00000356080 ; ENSP00000348381 ; ENSG00000148700 . [Q9UEY8-1 ]
    ENST00000360162 ; ENSP00000353286 ; ENSG00000148700 . [Q9UEY8-2 ]
    GeneIDi 120.
    KEGGi hsa:120.
    UCSCi uc001kys.4. human. [Q9UEY8-2 ]
    uc001kyt.4. human. [Q9UEY8-1 ]

    Organism-specific databases

    CTDi 120.
    GeneCardsi GC10P111755.
    H-InvDB HIX0170444.
    HGNCi HGNC:245. ADD3.
    HPAi CAB009797.
    HPA035696.
    MIMi 601568. gene.
    neXtProti NX_Q9UEY8.
    Orphaneti 210141. Inherited congenital spastic tetraplegia.
    PharmGKBi PA24567.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0235.
    HOGENOMi HOG000116349.
    HOVERGENi HBG004180.
    InParanoidi Q9UEY8.
    OMAi VNVPEES.
    OrthoDBi EOG7HF1HR.
    PhylomeDBi Q9UEY8.
    TreeFami TF313003.

    Miscellaneous databases

    ChiTaRSi ADD3. human.
    GeneWikii ADD3.
    GenomeRNAii 120.
    NextBioi 481.
    PMAP-CutDB Q9UEY8.
    PROi Q9UEY8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UEY8.
    Bgeei Q9UEY8.
    CleanExi HS_ADD3.
    Genevestigatori Q9UEY8.

    Family and domain databases

    Gene3Di 3.40.225.10. 1 hit.
    InterProi IPR027772. ADD3.
    IPR001303. Aldolase_II/adducin_N.
    [Graphical view ]
    PANTHERi PTHR10672:SF5. PTHR10672:SF5. 1 hit.
    Pfami PF00596. Aldolase_II. 1 hit.
    [Graphical view ]
    SMARTi SM01007. Aldolase_II. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53639. SSF53639. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression and chromosome mapping of adducin-like 70 (ADDL), a human cDNA highly homologous to human erythrocyte adducin."
      Katagiri T., Ozaki K., Fujiwara T., Shimizu F., Kawai A., Okuno S., Suzuki M., Nakamura Y., Takahashi E., Hirai Y.
      Cytogenet. Cell Genet. 74:90-95(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    2. "Cloning in the gamma quadrant."
      Moorthy S., Bennett V.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Endometrium.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Ovary.
    8. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
      Gocke C.B., Yu H., Kang J.
      J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-423; SER-442; SER-673; SER-677 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "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-402; SER-423 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-673 AND SER-677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-677 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiADDG_HUMAN
    AccessioniPrimary (citable) accession number: Q9UEY8
    Secondary accession number(s): D3DRA8
    , O43243, Q5VU09, Q92773, Q9UEY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3