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Protein

Syntenin-1

Gene

SDCBP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 heterodimerization activity Source: UniProtKB
  6. protein N-terminus binding Source: UniProtKB
  7. syndecan binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. axon guidance Source: Reactome
  3. ephrin receptor signaling pathway Source: Reactome
  4. intracellular signal transduction Source: UniProtKB
  5. positive regulation of exosomal secretion Source: UniProtKB
  6. positive regulation of extracellular vesicular exosome assembly Source: UniProtKB
  7. positive regulation of JNK cascade Source: BHF-UCL
  8. positive regulation of phosphorylation Source: BHF-UCL
  9. protein targeting to membrane Source: UniProtKB
  10. Ras protein signal transduction Source: Ensembl
  11. substrate-dependent cell migration, cell extension Source: UniProtKB
  12. synaptic transmission Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_22312. Neurofascin interactions.
REACT_264047. Ephrin signaling.
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 Componenti: 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: UniProtKB
  3. cytoplasm Source: BHF-UCL
  4. cytoskeleton Source: UniProtKB
  5. cytosol Source: Reactome
  6. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  7. extracellular space Source: UniProtKB
  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
  15. vesicle Source: UniProtKB
Complete GO annotation...

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
Modified residuei46 – 461Phosphotyrosine1 Publication

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

BgeeiO00560.
CleanExiHS_SDCBP.
ExpressionAtlasiO00560. baseline and differential.
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. 179 interactions.
DIPiDIP-42705N.
IntActiO00560. 53 interactions.
MINTiMINT-5002159.
STRINGi9606.ENSP00000260130.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000014465.
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. AlignAdd to basket

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

        10         20         30         40         50
MSLYPSLEDL KVDKVIQAQT AFSANPANPA ILSEASAPIP HDGNLYPRLY
60 70 80 90 100
PELSQYMGLS LNEEEIRANV AVVSGAPLQG QLVARPSSIN YMVAPVTGND
110 120 130 140 150
VGIRRAEIKQ GIREVILCKD QDGKIGLRLK SIDNGIFVQL VQANSPASLV
160 170 180 190 200
GLRFGDQVLQ INGENCAGWS SDKAHKVLKQ AFGEKITMTI RDRPFERTIT
210 220 230 240 250
MHKDSTGHVG FIFKNGKITS IVKDSSAARN GLLTEHNICE INGQNVIGLK
260 270 280 290
DSQIADILST SGTVVTITIM PAFIFEHIIK RMAPSIMKSL MDHTIPEV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi112287. 179 interactions.
DIPiDIP-42705N.
IntActiO00560. 53 interactions.
MINTiMINT-5002159.
STRINGi9606.ENSP00000260130.

PTM databases

PhosphoSiteiO00560.

Proteomic databases

MaxQBiO00560.
PaxDbiO00560.
PRIDEiO00560.

Protocols and materials databases

DNASUi6386.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi6386.
GeneCardsiGC08P059515.
HGNCiHGNC:10662. SDCBP.
HPAiCAB012245.
HPA023840.
MIMi602217. gene.
neXtProtiNX_O00560.
PharmGKBiPA35592.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG140434.
GeneTreeiENSGT00390000014465.
HOGENOMiHOG000231604.
HOVERGENiHBG053211.
InParanoidiO00560.
KOiK17254.
OrthoDBiEOG75MVWZ.
PhylomeDBiO00560.
TreeFamiTF327131.

Enzyme and pathway databases

ReactomeiREACT_22312. Neurofascin interactions.
REACT_264047. Ephrin signaling.
SignaLinkiO00560.

Miscellaneous databases

ChiTaRSiSDCBP. human.
EvolutionaryTraceiO00560.
GeneWikiiSDCBP.
GenomeRNAii6386.
NextBioi24796.
PROiO00560.
SOURCEiSearch...

Gene expression databases

BgeeiO00560.
CleanExiHS_SDCBP.
ExpressionAtlasiO00560. baseline and differential.
GenevestigatoriO00560.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1995)
    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 (DEC-1996) 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(1997) [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(2003) [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(2005) [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(2003) [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 (JAN-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(1997) [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(1998) [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(1999) [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(2000) [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(2000) [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(2008) [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].
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 113-273.
  22. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 197-270 IN COMPLEXES WITH IL5RA AND SDC4.
  23. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.73 ANGSTROMS) OF 197-273.
  24. 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: April 1, 2015
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.