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O00560

- SDCB1_HUMAN

UniProt

O00560 - SDCB1_HUMAN

Protein

Syntenin-1

Gene

SDCBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Seems to function as an adapter protein. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.3 Publications

    GO - Molecular functioni

    1. cytoskeletal adaptor activity Source: UniProtKB
    2. frizzled binding Source: BHF-UCL
    3. identical protein binding Source: IntAct
    4. interleukin-5 receptor binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein heterodimerization activity Source: UniProtKB
    7. protein N-terminus binding Source: UniProtKB
    8. syndecan binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. axon guidance Source: Reactome
    3. intracellular signal transduction Source: UniProtKB
    4. positive regulation of JNK cascade Source: BHF-UCL
    5. positive regulation of phosphorylation Source: BHF-UCL
    6. protein targeting to membrane Source: UniProtKB
    7. Ras protein signal transduction Source: Ensembl
    8. substrate-dependent cell migration, cell extension Source: UniProtKB
    9. synaptic transmission Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_22312. Neurofascin interactions.
    SignaLinkiO00560.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Syntenin-1
    Alternative name(s):
    Melanoma differentiation-associated protein 9
    Short name:
    MDA-9
    Pro-TGF-alpha cytoplasmic domain-interacting protein 18
    Short name:
    TACIP18
    Scaffold protein Pbp1
    Syndecan-binding protein 1
    Gene namesi
    Name:SDCBP
    Synonyms:MDA9, SYCL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:10662. SDCBP.

    Subcellular locationi

    Cell junctionfocal adhesion. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Nucleus. Melanosome. Cytoplasmcytosol. Cytoplasmcytoskeleton
    Note: Mainly membrane-associated. Localized to adherens junctions, focal adhesions and endoplasmic reticulum. Colocalized with actin stress fibers. Also found in the nucleus. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB
    2. blood microparticle Source: UniProt
    3. cytoplasm Source: BHF-UCL
    4. cytoskeleton Source: UniProtKB
    5. cytosol Source: Reactome
    6. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    7. extracellular space Source: UniProt
    8. extracellular vesicular exosome Source: UniProtKB
    9. focal adhesion Source: UniProtKB-SubCell
    10. interleukin-5 receptor complex Source: UniProtKB
    11. melanosome Source: UniProtKB-SubCell
    12. membrane Source: UniProtKB
    13. nucleus Source: UniProtKB
    14. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35592.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 298297Syntenin-1PRO_0000184001Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications

    Post-translational modificationi

    Phosphorylated on tyrosine residues.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00560.
    PaxDbiO00560.
    PRIDEiO00560.

    PTM databases

    PhosphoSiteiO00560.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in fetal kidney, liver, lung and brain. In adult highest expression in heart and placenta.

    Inductioni

    By IFNG/IFN-gamma in melanoma cells.

    Gene expression databases

    ArrayExpressiO00560.
    BgeeiO00560.
    CleanExiHS_SDCBP.
    GenevestigatoriO00560.

    Organism-specific databases

    HPAiCAB012245.
    HPA023840.

    Interactioni

    Subunit structurei

    Monomer and homodimer By similarity. Interacts with SDC1, SDC2, SDC3, SDC4, NRXN2, EPHA7, EPHB1, NF2 isoform 1, TGFA and IL5RA. Interacts with neurofascin, SDCBP2 and PTPRJ By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-727004,EBI-727004
    FZD7O750844EBI-727004,EBI-746917

    Protein-protein interaction databases

    BioGridi112287. 27 interactions.
    DIPiDIP-42705N.
    IntActiO00560. 51 interactions.
    MINTiMINT-5002159.
    STRINGi9606.ENSP00000260130.

    Structurei

    Secondary structure

    1
    298
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi113 – 1186
    Beta strandi121 – 1233
    Beta strandi126 – 1327
    Beta strandi135 – 1417
    Helixi146 – 1494
    Beta strandi157 – 1615
    Helixi171 – 18010
    Beta strandi183 – 1919
    Beta strandi197 – 2026
    Beta strandi205 – 2084
    Beta strandi211 – 2144
    Beta strandi217 – 2215
    Helixi226 – 2305
    Beta strandi234 – 2418
    Helixi251 – 26010
    Beta strandi263 – 2719

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N99X-ray1.94A/B113-273[»]
    1NTEX-ray1.24A197-273[»]
    1OBXX-ray1.35A197-270[»]
    1OBYX-ray1.85A/B197-270[»]
    1OBZX-ray1.69A/B113-273[»]
    1R6JX-ray0.73A197-273[»]
    1V1TX-ray1.80A/B113-273[»]
    1W9EX-ray1.56A/B113-273[»]
    1W9OX-ray2.25A/B113-273[»]
    1W9QX-ray1.70A/B113-273[»]
    1YBOX-ray2.30A/B113-273[»]
    ProteinModelPortaliO00560.
    SMRiO00560. Positions 113-273.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00560.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini114 – 19380PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini198 – 27376PDZ 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 PDZ (DHR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG140434.
    HOGENOMiHOG000231604.
    HOVERGENiHBG053211.
    InParanoidiO00560.
    KOiK17254.
    OrthoDBiEOG75MVWZ.
    PhylomeDBiO00560.
    TreeFamiTF327131.

    Family and domain databases

    Gene3Di2.30.42.10. 2 hits.
    InterProiIPR001478. PDZ.
    [Graphical view]
    PfamiPF00595. PDZ. 2 hits.
    [Graphical view]
    SMARTiSM00228. PDZ. 2 hits.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 2 hits.
    PROSITEiPS50106. PDZ. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00560-1) [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

    MSLYPSLEDL KVDKVIQAQT AFSANPANPA ILSEASAPIP HDGNLYPRLY    50
    PELSQYMGLS LNEEEIRANV AVVSGAPLQG QLVARPSSIN YMVAPVTGND 100
    VGIRRAEIKQ GIREVILCKD QDGKIGLRLK SIDNGIFVQL VQANSPASLV 150
    GLRFGDQVLQ INGENCAGWS SDKAHKVLKQ AFGEKITMTI RDRPFERTIT 200
    MHKDSTGHVG FIFKNGKITS IVKDSSAARN GLLTEHNICE INGQNVIGLK 250
    DSQIADILST SGTVVTITIM PAFIFEHIIK RMAPSIMKSL MDHTIPEV 298
    Length:298
    Mass (Da):32,444
    Last modified:July 1, 1997 - v1
    Checksum:i574E1349F86F949F
    GO
    Isoform 2 (identifier: O00560-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         81-81: Missing.

    Show »
    Length:297
    Mass (Da):32,316
    Checksum:i67FED210EFB6EEF6
    GO
    Isoform 3 (identifier: O00560-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         12-17: Missing.

    Show »
    Length:292
    Mass (Da):31,762
    Checksum:i004BFE46AC4D9FBA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 621N → S in AAB51246. (PubMed:9391086)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261P → T.
    Corresponds to variant rs11550282 [ dbSNP | Ensembl ].
    VAR_053699
    Natural varianti69 – 691N → S.1 Publication
    Corresponds to variant rs1127509 [ dbSNP | Ensembl ].
    VAR_013160

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei12 – 176Missing in isoform 3. 1 PublicationVSP_038374
    Alternative sequencei81 – 811Missing in isoform 2. 1 PublicationVSP_038375

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006636 mRNA. Translation: AAC52050.1.
    AF000652 mRNA. Translation: AAB97144.1.
    U83463 mRNA. Translation: AAB51246.1.
    AK300647 mRNA. Translation: BAG62335.1.
    AK312274 mRNA. Translation: BAG35204.1.
    AC068522 Genomic DNA. No translation available.
    CH471068 Genomic DNA. Translation: EAW86814.1.
    BC113674 mRNA. Translation: AAI13675.1.
    BC113676 mRNA. Translation: AAI13677.1.
    BC143915 mRNA. Translation: AAI43916.1.
    BC143916 mRNA. Translation: AAI43917.1.
    CCDSiCCDS47862.1. [O00560-2]
    CCDS47863.1. [O00560-3]
    CCDS6172.1. [O00560-1]
    PIRiJC6537.
    RefSeqiNP_001007068.1. NM_001007067.1. [O00560-1]
    NP_001007069.1. NM_001007068.1. [O00560-3]
    NP_001007070.1. NM_001007069.1. [O00560-2]
    NP_001007071.1. NM_001007070.1. [O00560-2]
    NP_005616.2. NM_005625.3. [O00560-1]
    UniGeneiHs.200804.

    Genome annotation databases

    EnsembliENST00000260130; ENSP00000260130; ENSG00000137575. [O00560-1]
    ENST00000413219; ENSP00000411771; ENSG00000137575. [O00560-1]
    ENST00000424270; ENSP00000395351; ENSG00000137575. [O00560-3]
    ENST00000447182; ENSP00000409288; ENSG00000137575. [O00560-2]
    GeneIDi6386.
    KEGGihsa:6386.
    UCSCiuc003xtn.3. human. [O00560-1]
    uc003xto.3. human. [O00560-2]
    uc003xtp.3. human. [O00560-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006636 mRNA. Translation: AAC52050.1 .
    AF000652 mRNA. Translation: AAB97144.1 .
    U83463 mRNA. Translation: AAB51246.1 .
    AK300647 mRNA. Translation: BAG62335.1 .
    AK312274 mRNA. Translation: BAG35204.1 .
    AC068522 Genomic DNA. No translation available.
    CH471068 Genomic DNA. Translation: EAW86814.1 .
    BC113674 mRNA. Translation: AAI13675.1 .
    BC113676 mRNA. Translation: AAI13677.1 .
    BC143915 mRNA. Translation: AAI43916.1 .
    BC143916 mRNA. Translation: AAI43917.1 .
    CCDSi CCDS47862.1. [O00560-2 ]
    CCDS47863.1. [O00560-3 ]
    CCDS6172.1. [O00560-1 ]
    PIRi JC6537.
    RefSeqi NP_001007068.1. NM_001007067.1. [O00560-1 ]
    NP_001007069.1. NM_001007068.1. [O00560-3 ]
    NP_001007070.1. NM_001007069.1. [O00560-2 ]
    NP_001007071.1. NM_001007070.1. [O00560-2 ]
    NP_005616.2. NM_005625.3. [O00560-1 ]
    UniGenei Hs.200804.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N99 X-ray 1.94 A/B 113-273 [» ]
    1NTE X-ray 1.24 A 197-273 [» ]
    1OBX X-ray 1.35 A 197-270 [» ]
    1OBY X-ray 1.85 A/B 197-270 [» ]
    1OBZ X-ray 1.69 A/B 113-273 [» ]
    1R6J X-ray 0.73 A 197-273 [» ]
    1V1T X-ray 1.80 A/B 113-273 [» ]
    1W9E X-ray 1.56 A/B 113-273 [» ]
    1W9O X-ray 2.25 A/B 113-273 [» ]
    1W9Q X-ray 1.70 A/B 113-273 [» ]
    1YBO X-ray 2.30 A/B 113-273 [» ]
    ProteinModelPortali O00560.
    SMRi O00560. Positions 113-273.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112287. 27 interactions.
    DIPi DIP-42705N.
    IntActi O00560. 51 interactions.
    MINTi MINT-5002159.
    STRINGi 9606.ENSP00000260130.

    PTM databases

    PhosphoSitei O00560.

    Proteomic databases

    MaxQBi O00560.
    PaxDbi O00560.
    PRIDEi O00560.

    Protocols and materials databases

    DNASUi 6386.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260130 ; ENSP00000260130 ; ENSG00000137575 . [O00560-1 ]
    ENST00000413219 ; ENSP00000411771 ; ENSG00000137575 . [O00560-1 ]
    ENST00000424270 ; ENSP00000395351 ; ENSG00000137575 . [O00560-3 ]
    ENST00000447182 ; ENSP00000409288 ; ENSG00000137575 . [O00560-2 ]
    GeneIDi 6386.
    KEGGi hsa:6386.
    UCSCi uc003xtn.3. human. [O00560-1 ]
    uc003xto.3. human. [O00560-2 ]
    uc003xtp.3. human. [O00560-3 ]

    Organism-specific databases

    CTDi 6386.
    GeneCardsi GC08P059515.
    HGNCi HGNC:10662. SDCBP.
    HPAi CAB012245.
    HPA023840.
    MIMi 602217. gene.
    neXtProti NX_O00560.
    PharmGKBi PA35592.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG140434.
    HOGENOMi HOG000231604.
    HOVERGENi HBG053211.
    InParanoidi O00560.
    KOi K17254.
    OrthoDBi EOG75MVWZ.
    PhylomeDBi O00560.
    TreeFami TF327131.

    Enzyme and pathway databases

    Reactomei REACT_22312. Neurofascin interactions.
    SignaLinki O00560.

    Miscellaneous databases

    ChiTaRSi SDCBP. human.
    EvolutionaryTracei O00560.
    GeneWikii SDCBP.
    GenomeRNAii 6386.
    NextBioi 24796.
    PROi O00560.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00560.
    Bgeei O00560.
    CleanExi HS_SDCBP.
    Genevestigatori O00560.

    Family and domain databases

    Gene3Di 2.30.42.10. 2 hits.
    InterProi IPR001478. PDZ.
    [Graphical view ]
    Pfami PF00595. PDZ. 2 hits.
    [Graphical view ]
    SMARTi SM00228. PDZ. 2 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 2 hits.
    PROSITEi PS50106. PDZ. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a novel melanoma differentiation associated gene, mda-9, that is down-regulated during terminal cell differentiation."
      Lin J.J., Jiang H., Fisher P.B.
      Mol. Cell. Differ. 4:317-333(1996)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SDC2, VARIANT SER-69.
    3. "A new family of scaffold proteins."
      Burbelo P.D.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Melanoma differentiation associated gene-9, mda-9, is a human gamma interferon responsive gene."
      Lin J.J., Jiang H., Fisher P.B.
      Gene 207:105-110(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "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] (ISOFORMS 1 AND 3).
      Tissue: Rectum and Urinary bladder.
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    9. Bienvenut W.V., Sumpton D.P., Lilla S., Ozanne B.W.
      Submitted (FEB-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14; 218-229 AND 289-298, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Pre-B cell.
    10. "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands."
      Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N., Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.
      Neuron 21:1453-1463(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHB1 AND EPHA7.
    11. "A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface."
      Fernandez-Larrea J., Merlos-Suarez A., Urena J.M., Baselga J., Arribas J.
      Mol. Cell 3:423-433(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TGFA.
    12. "Syntenin-syndecan binding requires syndecan-synteny and the co-operation of both PDZ domains of syntenin."
      Grootjans J.J., Reekmans G., Ceulemans H., David G.
      J. Biol. Chem. 275:19933-19941(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNDECANS; NRXN2 AND EPHB1.
    13. Cited for: INTERACTION WITH NF2.
    14. "Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments."
      Zimmermann P., Tomatis D., Rosas M., Grootjans J.J., Leenaerts I., Degeest G., Reekmans G., Coomans C., David G.
      Mol. Biol. Cell 12:339-350(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein."
      Geijsen N., Uings I.J., Pals C., Armstrong J., McKinnon M., Raaijmakers J.A.M., Lammers J.-W., Koenderman L., Coffer P.J.
      Science 293:1136-1138(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IL5RA.
    16. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    17. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    18. "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].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "PDZ tandem of human syntenin: crystal structure and functional properties."
      Kang B.S., Cooper D.R., Jelen F., Devedjiev Y., Derewenda U., Dauter Z., Otlewski J., Derewenda Z.S.
      Structure 11:459-468(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 113-273.
    21. "Molecular roots of degenerate specificity in syntenin's PDZ2 domain: reassessment of the PDZ recognition paradigm."
      Kang B.S., Cooper D.R., Devedjiev Y., Derewenda U., Derewenda Z.S.
      Structure 11:845-853(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 197-270 IN COMPLEXES WITH IL5RA AND SDC4.
    22. "The PDZ2 domain of syntenin at ultra-high resolution: bridging the gap between macromolecular and small molecule crystallography."
      Kang B.S., Devedjiev Y., Derewenda U., Derewenda Z.S.
      J. Mol. Biol. 338:483-493(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (0.73 ANGSTROMS) OF 197-273.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 113-273 IN COMPLEXES WITH C-TERMINAL PEPTIDES FROM NEUREXIN; EPHB1 AND SDC4.

    Entry informationi

    Entry nameiSDCB1_HUMAN
    AccessioniPrimary (citable) accession number: O00560
    Secondary accession number(s): B2R5Q7
    , B4DUH3, B7ZLN2, O00173, O43391, Q14CP2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 151 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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