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Q9QZQ1

- AFAD_MOUSE

UniProt

Q9QZQ1 - AFAD_MOUSE

Protein

Afadin

Gene

Mllt4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (10 Jul 2007)
      Previous versions | rss
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    Functioni

    Belongs to an adhesion system, probably together with the E-cadherin-catenin system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). Nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. May play a key role in the organization of epithelial structures of the embryonic ectoderm.1 Publication

    GO - Molecular functioni

    1. cell adhesion molecule binding Source: BHF-UCL
    2. protein binding Source: MGI

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. signal transduction Source: InterPro

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Afadin
    Alternative name(s):
    Protein Af-6
    Gene namesi
    Name:Mllt4
    Synonyms:Af6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1314653. Mllt4.

    Subcellular locationi

    Cell junctionadherens junction
    Note: Not found at cell-matrix AJs.

    GO - Cellular componenti

    1. adherens junction Source: MGI
    2. apical part of cell Source: MGI
    3. cell-cell adherens junction Source: MGI
    4. cell-cell junction Source: MGI
    5. cell junction Source: MGI
    6. cytoplasm Source: MGI
    7. nucleus Source: Ensembl
    8. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell junction

    Pathology & Biotechi

    Disruption phenotypei

    Mice show developmental defects at stages during and after gastrulation, including disorganization of the ectoderm, impaired migration of the mesoderm and loss of somites and other structures derived from both the ectoderm and mesoderm. Cell-cell adherens juntions and tight junctions are improperly organized in the ectoderm-derived cells. No redundancy exists in the function of afadin during gastrulation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18201820AfadinPRO_0000215919Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei216 – 2161Phosphoserine1 Publication
    Modified residuei557 – 5571Phosphoserine1 Publication
    Modified residuei1107 – 11071Phosphoserine1 Publication
    Modified residuei1182 – 11821Phosphoserine1 Publication
    Modified residuei1232 – 12321PhosphothreonineBy similarity
    Modified residuei1719 – 17191PhosphoserineBy similarity
    Modified residuei1795 – 17951PhosphoserineBy similarity
    Modified residuei1803 – 18031N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9QZQ1.
    PaxDbiQ9QZQ1.
    PRIDEiQ9QZQ1.

    PTM databases

    PhosphoSiteiQ9QZQ1.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed only in a restricted set of epithelial structures during early embryogenesis.1 Publication

    Developmental stagei

    Highly expressed at restricted set of epithelial structures and highly concentrated at their junctional complex regions. At E6.5, localized at the most apical regions of cell-cell adhesion sites of the entire embryonic ectoderm; not detected in the extraembryonic regions. At E7.0, expressed in the primitive streak and the migrating paraxial mesoderm. At E7.5, highly expressed at the junctional complex regions in the primitive streak region (neuroepithelium) and the neural fold/grove region, but hardly detected in other areas of the ectoderm. By E8.5, highly expressed in the tail bud, somites and the paraxial mesoderm, concentrated at the junctional complex regions in neural tube, somites and pericardioperitoneal canal.1 Publication

    Gene expression databases

    ArrayExpressiQ9QZQ1.
    BgeeiQ9QZQ1.
    GenevestigatoriQ9QZQ1.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with F-actin, nectin and PVRL3/nectin-3. Essential for the association of nectin and E-cadherin. Isoform 2/s-afadin does not interact with F-actin. Interacts with ZO-1 and occludin, but probably in an indirect manner. Interacts with RIT1, RIT2, NRXN1 and BCR By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201438. 5 interactions.
    DIPiDIP-60737N.
    IntActiQ9QZQ1. 2 interactions.

    Structurei

    Secondary structure

    1
    1820
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi249 – 2524
    Turni255 – 2573
    Beta strandi259 – 2613
    Beta strandi264 – 2674
    Helixi274 – 28512
    Beta strandi288 – 2903
    Turni292 – 2943
    Beta strandi295 – 3017
    Beta strandi308 – 3114
    Beta strandi315 – 3173
    Helixi325 – 3306
    Helixi334 – 3363
    Beta strandi339 – 3457
    Helixi381 – 3833
    Beta strandi386 – 3905
    Beta strandi418 – 4203
    Beta strandi423 – 4275
    Beta strandi429 – 4313
    Beta strandi450 – 4578
    Beta strandi459 – 4646
    Beta strandi466 – 4683
    Beta strandi470 – 4745
    Beta strandi481 – 4833
    Beta strandi488 – 4914
    Turni492 – 4943
    Beta strandi495 – 5006
    Beta strandi1007 – 10137
    Beta strandi1015 – 10173
    Beta strandi1019 – 10268
    Beta strandi1031 – 104111
    Helixi1045 – 10495
    Beta strandi1057 – 10615
    Helixi1071 – 10799
    Beta strandi1083 – 10908

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WLNNMR-A381-502[»]
    1WXANMR-A246-348[»]
    3AXAX-ray2.78A/B1003-1095[»]
    ProteinModelPortaliQ9QZQ1.
    SMRiQ9QZQ1. Positions 42-135, 249-348, 381-502, 604-936, 1001-1096, 1507-1685.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QZQ1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 13395Ras-associating 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini246 – 348103Ras-associating 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini426 – 49267FHAAdd
    BLAST
    Domaini653 – 908256DilutePROSITE-ProRule annotationAdd
    BLAST
    Domaini1007 – 109387PDZPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili146 – 18641Sequence AnalysisAdd
    BLAST
    Coiled coili1410 – 144637Sequence AnalysisAdd
    BLAST
    Coiled coili1523 – 156139Sequence AnalysisAdd
    BLAST
    Coiled coili1593 – 166573Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi163 – 17513Glu/Lys-richAdd
    BLAST
    Compositional biasi1346 – 139247Pro-richAdd
    BLAST
    Compositional biasi1676 – 170631Pro-richAdd
    BLAST
    Compositional biasi1733 – 17364Poly-Glu

    Sequence similaritiesi

    Contains 1 dilute domain.PROSITE-ProRule annotation
    Contains 1 FHA domain.Curated
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
    Contains 2 Ras-associating domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG291597.
    GeneTreeiENSGT00390000010033.
    HOGENOMiHOG000008041.
    HOVERGENiHBG050463.
    InParanoidiQ9QZQ1.
    KOiK05702.
    OrthoDBiEOG7G4QDD.
    PhylomeDBiQ9QZQ1.
    TreeFamiTF350731.

    Family and domain databases

    Gene3Di2.30.42.10. 1 hit.
    2.60.200.20. 1 hit.
    InterProiIPR018444. Dil_domain.
    IPR002710. Dilute.
    IPR000253. FHA_dom.
    IPR001478. PDZ.
    IPR000159. Ras-assoc.
    IPR008984. SMAD_FHA_domain.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF01843. DIL. 1 hit.
    PF00498. FHA. 1 hit.
    PF00595. PDZ. 1 hit.
    PF00788. RA. 2 hits.
    [Graphical view]
    SMARTiSM00240. FHA. 1 hit.
    SM00228. PDZ. 1 hit.
    SM00314. RA. 2 hits.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF54236. SSF54236. 2 hits.
    PROSITEiPS51126. DILUTE. 1 hit.
    PS50106. PDZ. 1 hit.
    PS50200. RA. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 3 (identifier: Q9QZQ1-3) [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

    MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK     50
    AAGNFATKCI RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG 100
    ERRLDIDEKP LVVQLNWNKD DREGRFVLKN ENDAIPAKKA QSNGPEKQEK 150
    EGVIQNFKRT LSKKEKKEKK KKEKEALRQA SDKEERPSQG DDSENSRLAA 200
    EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS DGRPDSGGTL 250
    RIYADSLKPN IPYKTILLST TDTADFAVAE SLEKYGLEKE NPKDYCIARV 300
    MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY 350
    IPKKMKKHVE GKSLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY 400
    YSYHTYEDGS DSRDKPKLYR LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC 450
    DLTNMDGVVT VTPRSMDAET YVDGQRISET TMLQSGMRLQ FGTSHVFKFV 500
    DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDV HSGTALPASR 550
    STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQEYRRRENR TQDATGPELI 600
    LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH 650
    RPDISPTERT HKAIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN 700
    FIKQDRDLSR ITLDAQDVLA HLVQMAFKYL VHCLQSELNN YMPAFLDDPE 750
    ENSLQRPKID DVLHTLTGAM SLLRRCRVNA ALTIQLFSQL FHFINMWLFN 800
    RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD CHLSRIVQAT 850
    TLLTMDKYVP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE 900
    NVVAVAENTA DELARSDGRD VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN 950
    GLQEFLDPLC QRGFCRLVPH TRSPGTWTIY FEGADYESHL MRENAELAQP 1000
    LRKEPEIITV TLKKQNGMGL SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG 1050
    RLAAGDQLLS VDGRSLVGLS QERAAELMTR TSSVVTLEVA KQGAIYHGLA 1100
    TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS PESPQMPWTE 1150
    YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKGPYT SGTAAKITSV 1200
    STGNLCTEEQ SPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQSQWP 1250
    NYEEKPHVHT ESNHSSIAIQ RVTRSQEELR EEKVYQLERH RVEAGMDRKC 1300
    DSDMWINQSS SVESSTSSQE HLNHSSKSVT PASTLTKSGP GRWKTPAAVL 1350
    PTPVAVSQPI RTDLPPPPPP PPVHYTSEFD GIPMDLPLPP PPANQAGPQS 1400
    AQVAAAEWKK REEHQRWYEK EKARLEEERE RKRREQERKL GQMRSQTLNP 1450
    ASFSPLATQA KPEKPSTLQR PQETVIRELQ PQQQPRTIER KDLQYITISK 1500
    EELSSGDSLS PDPWKRDARE KLEKQQQMHI VDMLSKEIHE LQNKVDRTAE 1550
    ESDRLRKLML EWQFQKRLQE SKQKDEDDDE EEDDDVDTML IMQRLEAERR 1600
    ARMQDEERRR QQQLEEMRKR EAEDRVRQEE DGRHQEEERV KRDAEEKRRQ 1650
    EEGYYSRLEA ERRRQHEEAA RRLLEPEEPG LSRPPLPRDY EPPSLSSAPC 1700
    APPPPPQRNA SYLKTQVLSP DSLFTAKFVA YDEEEEDYGP AGPNSYSGSA 1750
    GTAVGAYDAP REAREKLTRS QDADLPGSSG APENLTFKER QRLFSQGQDV 1800
    SDKVKASRKL TELENELNTK 1820
    Length:1,820
    Mass (Da):206,499
    Last modified:July 10, 2007 - v3
    Checksum:i9FA4F378D840D8B1
    GO
    Isoform 1 (identifier: Q9QZQ1-2) [UniParc]FASTAAdd to Basket

    Also known as: l-afadin

    The sequence of this isoform differs from the canonical sequence as follows:
         393-407: Missing.

    Show »
    Length:1,805
    Mass (Da):204,553
    Checksum:i5987A16BA9F28C2E
    GO
    Isoform 2 (identifier: Q9QZQ1-1)

    Also known as: s-afadin

    Sequence is not available
    Length:
    Mass (Da):

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231N → Y in AAD54283. (PubMed:10477764)Curated
    Sequence conflicti101 – 1011E → EE in AK016557. (PubMed:16141072)Curated
    Sequence conflicti694 – 6941N → D in AK016557. (PubMed:16141072)Curated
    Sequence conflicti897 – 9004DLIE → PEMR in AK016557. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei393 – 40715Missing in isoform 1. 1 PublicationVSP_026731Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC155253 Genomic DNA. No translation available.
    CAAA01106165 Genomic DNA. No translation available.
    CAAA01134612 Genomic DNA. No translation available.
    CAAA01201738 Genomic DNA. No translation available.
    CAAA01218165 Genomic DNA. No translation available.
    AF172447 mRNA. Translation: AAD54283.1.
    AK016557 mRNA. No translation available.
    CCDSiCCDS49955.1. [Q9QZQ1-3]
    RefSeqiNP_034936.1. NM_010806.1. [Q9QZQ1-3]
    UniGeneiMm.59167.

    Genome annotation databases

    EnsembliENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036. [Q9QZQ1-3]
    ENSMUST00000150848; ENSMUSP00000122447; ENSMUSG00000068036. [Q9QZQ1-2]
    GeneIDi17356.
    KEGGimmu:17356.
    UCSCiuc008amr.1. mouse. [Q9QZQ1-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC155253 Genomic DNA. No translation available.
    CAAA01106165 Genomic DNA. No translation available.
    CAAA01134612 Genomic DNA. No translation available.
    CAAA01201738 Genomic DNA. No translation available.
    CAAA01218165 Genomic DNA. No translation available.
    AF172447 mRNA. Translation: AAD54283.1 .
    AK016557 mRNA. No translation available.
    CCDSi CCDS49955.1. [Q9QZQ1-3 ]
    RefSeqi NP_034936.1. NM_010806.1. [Q9QZQ1-3 ]
    UniGenei Mm.59167.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WLN NMR - A 381-502 [» ]
    1WXA NMR - A 246-348 [» ]
    3AXA X-ray 2.78 A/B 1003-1095 [» ]
    ProteinModelPortali Q9QZQ1.
    SMRi Q9QZQ1. Positions 42-135, 249-348, 381-502, 604-936, 1001-1096, 1507-1685.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201438. 5 interactions.
    DIPi DIP-60737N.
    IntActi Q9QZQ1. 2 interactions.

    PTM databases

    PhosphoSitei Q9QZQ1.

    Proteomic databases

    MaxQBi Q9QZQ1.
    PaxDbi Q9QZQ1.
    PRIDEi Q9QZQ1.

    Protocols and materials databases

    DNASUi 17356.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000139666 ; ENSMUSP00000118318 ; ENSMUSG00000068036 . [Q9QZQ1-3 ]
    ENSMUST00000150848 ; ENSMUSP00000122447 ; ENSMUSG00000068036 . [Q9QZQ1-2 ]
    GeneIDi 17356.
    KEGGi mmu:17356.
    UCSCi uc008amr.1. mouse. [Q9QZQ1-3 ]

    Organism-specific databases

    CTDi 4301.
    MGIi MGI:1314653. Mllt4.

    Phylogenomic databases

    eggNOGi NOG291597.
    GeneTreei ENSGT00390000010033.
    HOGENOMi HOG000008041.
    HOVERGENi HBG050463.
    InParanoidi Q9QZQ1.
    KOi K05702.
    OrthoDBi EOG7G4QDD.
    PhylomeDBi Q9QZQ1.
    TreeFami TF350731.

    Miscellaneous databases

    ChiTaRSi MLLT4. mouse.
    EvolutionaryTracei Q9QZQ1.
    NextBioi 291962.
    PROi Q9QZQ1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QZQ1.
    Bgeei Q9QZQ1.
    Genevestigatori Q9QZQ1.

    Family and domain databases

    Gene3Di 2.30.42.10. 1 hit.
    2.60.200.20. 1 hit.
    InterProi IPR018444. Dil_domain.
    IPR002710. Dilute.
    IPR000253. FHA_dom.
    IPR001478. PDZ.
    IPR000159. Ras-assoc.
    IPR008984. SMAD_FHA_domain.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF01843. DIL. 1 hit.
    PF00498. FHA. 1 hit.
    PF00595. PDZ. 1 hit.
    PF00788. RA. 2 hits.
    [Graphical view ]
    SMARTi SM00240. FHA. 1 hit.
    SM00228. PDZ. 1 hit.
    SM00314. RA. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    SSF50156. SSF50156. 1 hit.
    SSF54236. SSF54236. 2 hits.
    PROSITEi PS51126. DILUTE. 1 hit.
    PS50106. PDZ. 1 hit.
    PS50200. RA. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "Afadin: a key molecule essential for structural organization of cell-cell junctions of polarized epithelia during embryogenesis."
      Ikeda W., Nakanishi H., Miyoshi J., Mandai K., Ishizaki H., Tanaka M., Togawa A., Takahashi K., Nishioka H., Yoshida H., Mizoguchi A., Nishikawa S., Takai Y.
      J. Cell Biol. 146:1117-1132(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-320 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
      Strain: C57BL/6.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-900 (ISOFORM 3).
      Tissue: Leukemia.
    4. "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities."
      Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M., Tachibana K., Mizoguchi A., Takai Y.
      J. Biol. Chem. 275:10291-10299(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PVRL3.
    5. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    10. "Solution structure of the FHA domain and RAS-binding domain in mouse AF-6 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 246-487.

    Entry informationi

    Entry nameiAFAD_MOUSE
    AccessioniPrimary (citable) accession number: Q9QZQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 113 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3