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Q5TCZ1

- SPD2A_HUMAN

UniProt

Q5TCZ1 - SPD2A_HUMAN

Protein

SH3 and PX domain-containing protein 2A

Gene

SH3PXD2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of beta-amyloid peptide.5 Publications

    GO - Molecular functioni

    1. phosphatidylinositol binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. superoxide metabolic process Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SH3 and PX domain-containing protein 2A
    Alternative name(s):
    Adapter protein TKS5
    Five SH3 domain-containing protein
    SH3 multiple domains protein 1
    Tyrosine kinase substrate with five SH3 domains
    Gene namesi
    Name:SH3PXD2A
    Synonyms:FISH, KIAA0418, SH3MD1, TKS5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:23664. SH3PXD2A.

    Subcellular locationi

    Cytoplasm. Cell projectionpodosome
    Note: Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cell projection Source: UniProtKB-KW
    3. cytoplasm Source: UniProtKB-SubCell
    4. podosome Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421R → A: Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2). 1 Publication
    Mutagenesisi93 – 931R → A: Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2). 1 Publication

    Organism-specific databases

    PharmGKBiPA134956816.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11331133SH3 and PX domain-containing protein 2APRO_0000278488Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei421 – 4211Phosphoserine1 Publication
    Modified residuei547 – 5471Phosphoserine1 Publication
    Modified residuei567 – 5671Phosphoserine1 Publication
    Modified residuei593 – 5931Phosphoserine1 Publication
    Modified residuei644 – 6441Phosphoserine1 Publication
    Modified residuei731 – 7311Phosphothreonine1 Publication
    Modified residuei819 – 8191PhosphoserineBy similarity
    Modified residuei1002 – 10021Phosphoserine2 Publications
    Modified residuei1016 – 10161Phosphoserine1 Publication
    Modified residuei1017 – 10171Phosphoserine1 Publication
    Modified residuei1038 – 10381Phosphoserine1 Publication

    Post-translational modificationi

    Tyrosine phosphorylated by SRC. Phosphorylation plays a regulatory role in the protein localization. The intramolecular interaction of the PX domain with the third SH3 domain maintains the protein in the cytoplasm and phosphorylation disrupts this interaction, resulting in the redistribution of the protein from cytoplasm to the perimembrane region. Phosphorylated on serine upon DNA damage, probably by ATM or ATR.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5TCZ1.
    PaxDbiQ5TCZ1.
    PRIDEiQ5TCZ1.

    PTM databases

    PhosphoSiteiQ5TCZ1.

    Expressioni

    Tissue specificityi

    Found in several cancer cell lines, particularly invasive breast carcinomas and melanomas.1 Publication

    Gene expression databases

    ArrayExpressiQ5TCZ1.
    BgeeiQ5TCZ1.
    CleanExiHS_SH3PXD2A.
    GenevestigatoriQ5TCZ1.

    Organism-specific databases

    HPAiHPA037922.
    HPA037923.

    Interactioni

    Subunit structurei

    Interacts (via N-terminus) with CYBA By similarity. Interacts with ADAM12, ADAM15 and ADAM19. Interacts with NOXO1. Interacts (via SH3 domains) with NOXA1. Interacts with FASLG.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAM15Q134442EBI-2483234,EBI-77818
    Dnm1P215752EBI-7014859,EBI-80070From a different organism.
    SOS1Q078895EBI-7014859,EBI-297487

    Protein-protein interaction databases

    BioGridi115002. 11 interactions.
    IntActiQ5TCZ1. 12 interactions.
    MINTiMINT-2792114.
    STRINGi9606.ENSP00000348215.

    Structurei

    Secondary structure

    1
    1133
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi181 – 1844
    Beta strandi194 – 1985
    Beta strandi202 – 2076
    Beta strandi212 – 2165
    Helixi217 – 2193
    Beta strandi221 – 2233
    Beta strandi268 – 2725
    Beta strandi292 – 2954
    Beta strandi300 – 3089
    Beta strandi311 – 3166
    Helixi317 – 3193
    Beta strandi843 – 8475
    Beta strandi866 – 8727
    Beta strandi876 – 8827
    Beta strandi885 – 8906
    Turni891 – 8933
    Beta strandi1075 – 10795
    Beta strandi1087 – 10893
    Beta strandi1097 – 11004
    Beta strandi1107 – 11137
    Beta strandi1116 – 11183
    Beta strandi1120 – 11256
    Helixi1126 – 11283
    Beta strandi1129 – 11313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DNUNMR-A268-325[»]
    2EGANMR-A168-224[»]
    2EGCNMR-A1072-1133[»]
    2EKHNMR-A842-908[»]
    ProteinModelPortaliQ5TCZ1.
    SMRiQ5TCZ1. Positions 6-126, 162-329, 448-506, 842-908, 1072-1133.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5TCZ1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 128125PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini166 – 22560SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini266 – 32560SH3 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini448 – 50760SH3 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini840 – 89960SH3 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1071 – 113363SH3 5PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili917 – 94630Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi634 – 72491Ser-richAdd
    BLAST

    Domaini

    The PX domain is required for podosome localization because of its ability to bind phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-phosphate (PtdIns4P), phosphatidylinositol 5-phosphate (PtdIns5P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain By similarity.By similarity
    The fifth SH3 domain mediates binding with ADAM12, ADAM15 and ADAM19.2 Publications

    Sequence similaritiesi

    Belongs to the SH3PXD2 family.Curated
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation
    Contains 5 SH3 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG148927.
    HOGENOMiHOG000154376.
    HOVERGENiHBG089589.
    InParanoidiQ5TCZ1.
    OMAiLESGWWY.
    OrthoDBiEOG7H4DSQ.
    PhylomeDBiQ5TCZ1.
    TreeFamiTF329347.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR001683. Phox.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF00787. PX. 1 hit.
    PF00018. SH3_1. 4 hits.
    [Graphical view]
    SMARTiSM00312. PX. 1 hit.
    SM00326. SH3. 5 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 5 hits.
    SSF64268. SSF64268. 1 hit.
    PROSITEiPS50195. PX. 1 hit.
    PS50002. SH3. 5 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5TCZ1-1) [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

    MLAYCVQDAT VVDVEKRRNP SKHYVYIINV TWSDSTSQTI YRRYSKFFDL     50
    QMQLLDKFPI EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA VKRLKPIDEY 100
    CRALVRLPPH ISQCDEVFRF FEARPEDVNP PKEDYGSSKR KSVWLSSWAE 150
    SPKKDVTGAD ATAEPMILEQ YVVVSNYKKQ ENSELSLQAG EVVDVIEKNE 200
    SGWWFVSTSE EQGWVPATYL EAQNGTRDDS DINTSKTGEV SKRRKAHLRR 250
    LDRRWTLGGM VNRQHSREEK YVTVQPYTSQ SKDEIGFEKG VTVEVIRKNL 300
    EGWWYIRYLG KEGWAPASYL KKAKDDLPTR KKNLAGPVEI IGNIMEISNL 350
    LNKKASGDKE TPPAEGEGHE APIAKKEISL PILCNASNGS AVGVPDRTVS 400
    RLAQGSPAVA RIAPQRAQIS SPNLRTRPPP RRESSLGFQL PKPPEPPSVE 450
    VEYYTIAEFQ SCISDGISFR GGQKAEVIDK NSGGWWYVQI GEKEGWAPAS 500
    YIDKRKKPNL SRRTSTLTRP KVPPPAPPSK PKEAEEGPTG ASESQDSPRK 550
    LKYEEPEYDI PAFGFDSEPE LSEEPVEDRA SGERRPAQPH RPSPASSLQR 600
    ARFKVGESSE DVALEEETIY ENEGFRPYAE DTLSARGSSG DSDSPGSSSL 650
    SLTRKNSPKS GSPKSSSLLK LKAEKNAQAE MGKNHSSASF SSSITINTTC 700
    CSSSSSSSSS LSKTSGDLKP RSASDAGIRG TPKVRAKKDA DANAGLTSCP 750
    RAKPSVRPKP FLNRAESQSQ EKMDISTLRR QLRPTGQLRG GLKGSKSEDS 800
    ELPPQTASEA PSEGSRRSSS DLITLPATTP PCPTKKEWEG PATSYMTCSA 850
    YQKVQDSEIS FPAGVEVQVL EKQESGWWYV RFGELEGWAP SHYLVLDENE 900
    QPDPSGKELD TVPAKGRQNE GKSDSLEKIE RRVQALNTVN QSKKATPPIP 950
    SKPPGGFGKT SGTPAVKMRN GVRQVAVRPQ SVFVSPPPKD NNLSCALRRN 1000
    ESLTATDGLR GVRRNSSFST ARSAAAEAKG RLAERAASQG SDSPLLPAQR 1050
    NSIPVSPVRP KPIEKSQFIH NNLKDVYVSI ADYEGDEETA GFQEGVSMEV 1100
    LERNPNGWWY CQILDGVKPF KGWVPSNYLE KKN 1133
    Length:1,133
    Mass (Da):125,289
    Last modified:December 21, 2004 - v1
    Checksum:iD485F49E9192359C
    GO
    Isoform 2 (identifier: Q5TCZ1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-165: Missing.
         240-267: Missing.

    Show »
    Length:940
    Mass (Da):102,618
    Checksum:i1CA24D7BC03B8AC3
    GO
    Isoform 3 (identifier: Q5TCZ1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         240-267: Missing.

    Note: Gene prediction based on similarity to mouse ortholog and partial transcript data.

    Show »
    Length:1,105
    Mass (Da):121,836
    Checksum:i384ECB9785EE3FAB
    GO

    Sequence cautioni

    The sequence BAA24848.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti659 – 6591K → Q.
    Corresponds to variant rs11818820 [ dbSNP | Ensembl ].
    VAR_030781
    Natural varianti1035 – 10351R → Q.
    Corresponds to variant rs3781365 [ dbSNP | Ensembl ].
    VAR_030782
    Natural varianti1073 – 10731L → P.
    Corresponds to variant rs12764700 [ dbSNP | Ensembl ].
    VAR_056993

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 165165Missing in isoform 2. 1 PublicationVSP_023312Add
    BLAST
    Alternative sequencei240 – 26728Missing in isoform 2 and isoform 3. 1 PublicationVSP_023313Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007878 mRNA. Translation: BAA24848.2. Different initiation.
    AL121929, AL133355 Genomic DNA. Translation: CAI13961.1.
    AL121929, AL133355 Genomic DNA. Translation: CAI13962.1.
    AL121929 Genomic DNA. Translation: CAI13963.1.
    AL133355, AL121929 Genomic DNA. Translation: CAI15351.1.
    AL133355, AL121929 Genomic DNA. Translation: CAI15352.1.
    CH471066 Genomic DNA. Translation: EAW49623.1.
    CH471066 Genomic DNA. Translation: EAW49624.1.
    CCDSiCCDS31278.1. [Q5TCZ1-3]
    PIRiT00056.
    RefSeqiNP_055446.2. NM_014631.2. [Q5TCZ1-3]
    XP_005270351.1. XM_005270294.2. [Q5TCZ1-1]
    UniGeneiHs.678727.

    Genome annotation databases

    EnsembliENST00000355946; ENSP00000348215; ENSG00000107957. [Q5TCZ1-3]
    ENST00000369774; ENSP00000358789; ENSG00000107957. [Q5TCZ1-1]
    GeneIDi9644.
    KEGGihsa:9644.
    UCSCiuc001kxj.1. human. [Q5TCZ1-3]
    uc009xxn.1. human. [Q5TCZ1-2]
    uc010qqu.1. human. [Q5TCZ1-1]

    Polymorphism databases

    DMDMi74746151.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007878 mRNA. Translation: BAA24848.2 . Different initiation.
    AL121929 , AL133355 Genomic DNA. Translation: CAI13961.1 .
    AL121929 , AL133355 Genomic DNA. Translation: CAI13962.1 .
    AL121929 Genomic DNA. Translation: CAI13963.1 .
    AL133355 , AL121929 Genomic DNA. Translation: CAI15351.1 .
    AL133355 , AL121929 Genomic DNA. Translation: CAI15352.1 .
    CH471066 Genomic DNA. Translation: EAW49623.1 .
    CH471066 Genomic DNA. Translation: EAW49624.1 .
    CCDSi CCDS31278.1. [Q5TCZ1-3 ]
    PIRi T00056.
    RefSeqi NP_055446.2. NM_014631.2. [Q5TCZ1-3 ]
    XP_005270351.1. XM_005270294.2. [Q5TCZ1-1 ]
    UniGenei Hs.678727.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DNU NMR - A 268-325 [» ]
    2EGA NMR - A 168-224 [» ]
    2EGC NMR - A 1072-1133 [» ]
    2EKH NMR - A 842-908 [» ]
    ProteinModelPortali Q5TCZ1.
    SMRi Q5TCZ1. Positions 6-126, 162-329, 448-506, 842-908, 1072-1133.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115002. 11 interactions.
    IntActi Q5TCZ1. 12 interactions.
    MINTi MINT-2792114.
    STRINGi 9606.ENSP00000348215.

    PTM databases

    PhosphoSitei Q5TCZ1.

    Polymorphism databases

    DMDMi 74746151.

    Proteomic databases

    MaxQBi Q5TCZ1.
    PaxDbi Q5TCZ1.
    PRIDEi Q5TCZ1.

    Protocols and materials databases

    DNASUi 9644.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355946 ; ENSP00000348215 ; ENSG00000107957 . [Q5TCZ1-3 ]
    ENST00000369774 ; ENSP00000358789 ; ENSG00000107957 . [Q5TCZ1-1 ]
    GeneIDi 9644.
    KEGGi hsa:9644.
    UCSCi uc001kxj.1. human. [Q5TCZ1-3 ]
    uc009xxn.1. human. [Q5TCZ1-2 ]
    uc010qqu.1. human. [Q5TCZ1-1 ]

    Organism-specific databases

    CTDi 9644.
    GeneCardsi GC10M105345.
    HGNCi HGNC:23664. SH3PXD2A.
    HPAi HPA037922.
    HPA037923.
    neXtProti NX_Q5TCZ1.
    PharmGKBi PA134956816.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148927.
    HOGENOMi HOG000154376.
    HOVERGENi HBG089589.
    InParanoidi Q5TCZ1.
    OMAi LESGWWY.
    OrthoDBi EOG7H4DSQ.
    PhylomeDBi Q5TCZ1.
    TreeFami TF329347.

    Miscellaneous databases

    ChiTaRSi SH3PXD2A. human.
    EvolutionaryTracei Q5TCZ1.
    GeneWikii SH3PXD2A.
    GenomeRNAii 9644.
    NextBioi 36199.
    PROi Q5TCZ1.

    Gene expression databases

    ArrayExpressi Q5TCZ1.
    Bgeei Q5TCZ1.
    CleanExi HS_SH3PXD2A.
    Genevestigatori Q5TCZ1.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR001683. Phox.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF00787. PX. 1 hit.
    PF00018. SH3_1. 4 hits.
    [Graphical view ]
    SMARTi SM00312. PX. 1 hit.
    SM00326. SH3. 5 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 5 hits.
    SSF64268. SSF64268. 1 hit.
    PROSITEi PS50195. PX. 1 hit.
    PS50002. SH3. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
      Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. Okazaki N., Kikuno R.F., Nagase T., Ohara O., Koga H.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
      Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., Courtneidge S.A.
      J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH ADAM12; ADAM15 AND ADAM19, MUTAGENESIS OF ARG-42 AND ARG-93.
    6. "The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells."
      Seals D.F., Azucena E.F. Jr., Pass I., Tesfay L., Gordon R., Woodrow M., Resau J.H., Courtneidge S.A.
      Cancer Cell 7:155-165(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY.
    7. "Amyloid-beta neurotoxicity is mediated by FISH adapter protein and ADAM12 metalloprotease activity."
      Malinin N.L., Wright S., Seubert P., Schenk D., Griswold-Prenner I.
      Proc. Natl. Acad. Sci. U.S.A. 102:3058-3063(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADAM12, PTM.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "A role for the podosome/invadopodia scaffold protein Tks5 in tumor growth in vivo."
      Blouw B., Seals D.F., Pass I., Diaz B., Courtneidge S.A.
      Eur. J. Cell Biol. 87:555-567(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421; SER-547; SER-567; SER-593; SER-644; THR-731; SER-1002; SER-1016; SER-1017 AND SER-1038, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    12. "Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity."
      Gianni D., Diaz B., Taulet N., Fowler B., Courtneidge S.A., Bokoch G.M.
      Sci. Signal. 2:RA54-RA54(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NOXA1.
    13. "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-1002, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation."
      Gianni D., Dermardirossian C., Bokoch G.M.
      Eur. J. Cell Biol. 90:164-171(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NOXA1 AND NOXO1.
    15. "Solution structure of the SH3 domains from human KIAA0418 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 168-325 AND 1072-1133.

    Entry informationi

    Entry nameiSPD2A_HUMAN
    AccessioniPrimary (citable) accession number: Q5TCZ1
    Secondary accession number(s): D3DR98
    , O43302, Q5TCZ2, Q5TDQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 102 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3