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O00560 (SDCB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SDCBP
Synonyms:MDA9, SYCL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.14 Ref.15

Subunit structure

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. Ref.2 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Subcellular location

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. Ref.14 Ref.16 Ref.17

Tissue specificity

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

Induction

By IFNG/IFN-gamma in melanoma cells.

Post-translational modification

Phosphorylated on tyrosine residues.

Sequence similarities

Contains 2 PDZ (DHR) domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Endoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton organization

Non-traceable author statement PubMed 12037664. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

intracellular signal transduction

Non-traceable author statement Ref.2. Source: UniProtKB

positive regulation of JNK cascade

Inferred by curator PubMed 18256285. Source: BHF-UCL

positive regulation of phosphorylation

Inferred from direct assay PubMed 18256285. Source: BHF-UCL

protein targeting to membrane

Non-traceable author statement Ref.11. Source: UniProtKB

substrate-dependent cell migration, cell extension

Non-traceable author statement PubMed 12037664. Source: UniProtKB

synaptic transmission

Non-traceable author statement Ref.10. Source: UniProtKB

   Cellular_componentadherens junction

Non-traceable author statement Ref.14. Source: UniProtKB

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytoplasm

Inferred from direct assay PubMed 18256285. Source: BHF-UCL

cytoskeleton

Non-traceable author statement Ref.2. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

interleukin-5 receptor complex

Inferred from sequence or structural similarity Ref.15. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Non-traceable author statement Ref.2. Source: UniProtKB

nucleus

Non-traceable author statement Ref.14. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 18256285. Source: BHF-UCL

   Molecular_functioncytoskeletal adaptor activity

Non-traceable author statement Ref.2. Source: UniProtKB

frizzled binding

Inferred from physical interaction PubMed 18256285. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 22673509. Source: IntAct

interleukin-5 receptor binding

Inferred from sequence or structural similarity Ref.15. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 15371445. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 11152476. Source: UniProtKB

syndecan binding

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-727004,EBI-727004
FZD7O750844EBI-727004,EBI-746917

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00560-1)

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.
Isoform 2 (identifier: O00560-2)

The sequence of this isoform differs from the canonical sequence as follows:
     81-81: Missing.
Isoform 3 (identifier: O00560-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 298297Syntenin-1
PRO_0000184001

Regions

Domain114 – 19380PDZ 1
Domain198 – 27376PDZ 2

Amino acid modifications

Modified residue21N-acetylserine Ref.9 Ref.18

Natural variations

Alternative sequence12 – 176Missing in isoform 3.
VSP_038374
Alternative sequence811Missing in isoform 2.
VSP_038375
Natural variant261P → T.
Corresponds to variant rs11550282 [ dbSNP | Ensembl ].
VAR_053699
Natural variant691N → S. Ref.2
Corresponds to variant rs1127509 [ dbSNP | Ensembl ].
VAR_013160

Experimental info

Sequence conflict621N → S in AAB51246. Ref.2

Secondary structure

................................. 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 574E1349F86F949F

FASTA29832,444
        10         20         30         40         50         60 
MSLYPSLEDL KVDKVIQAQT AFSANPANPA ILSEASAPIP HDGNLYPRLY PELSQYMGLS 

        70         80         90        100        110        120 
LNEEEIRANV AVVSGAPLQG QLVARPSSIN YMVAPVTGND VGIRRAEIKQ GIREVILCKD 

       130        140        150        160        170        180 
QDGKIGLRLK SIDNGIFVQL VQANSPASLV GLRFGDQVLQ INGENCAGWS SDKAHKVLKQ 

       190        200        210        220        230        240 
AFGEKITMTI RDRPFERTIT MHKDSTGHVG FIFKNGKITS IVKDSSAARN GLLTEHNICE 

       250        260        270        280        290 
INGQNVIGLK DSQIADILST SGTVVTITIM PAFIFEHIIK RMAPSIMKSL MDHTIPEV 

« Hide

Isoform 2 [UniParc].

Checksum: 67FED210EFB6EEF6
Show »

FASTA29732,316
Isoform 3 [UniParc].

Checksum: 004BFE46AC4D9FBA
Show »

FASTA29231,762

References

« Hide 'large scale' references
[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]"Syntenin, a PDZ protein that binds syndecan cytoplasmic domains."
Grootjans J.J., Zimmermann P., Reekmans G., Smets A., Degeest G., Duerr J., David G.
Proc. Natl. Acad. Sci. U.S.A. 94:13683-13688(1997) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Schwannomin isoform-1 interacts with syntenin via PDZ domains."
Jannatipour M., Dion P., Khan S., Jindal H., Fan X., Laganiere J., Chishti A.H., Rouleau G.A.
J. Biol. Chem. 276:33093-33100(2001) [PubMed] [Europe PMC] [Abstract]
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]"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins."
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E.
J. Proteome Res. 2:69-79(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[17]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The binding of the PDZ tandem of syntenin to target proteins."
Grembecka J., Cierpicki T., Devedjiev Y., Derewenda U., Kang B.S., Bushweller J.H., Derewenda Z.S.
Biochemistry 45:3674-3683(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 113-273 IN COMPLEXES WITH C-TERMINAL PEPTIDES FROM NEUREXIN; EPHB1 AND SDC4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC6537.
RefSeqNP_001007068.1. NM_001007067.1.
NP_001007069.1. NM_001007068.1.
NP_001007070.1. NM_001007069.1.
NP_001007071.1. NM_001007070.1.
NP_005616.2. NM_005625.3.
UniGeneHs.200804.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO00560.
SMRO00560. Positions 113-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112287. 25 interactions.
DIPDIP-42705N.
IntActO00560. 50 interactions.
MINTMINT-5002159.
STRING9606.ENSP00000260130.

PTM databases

PhosphoSiteO00560.

Proteomic databases

PaxDbO00560.
PRIDEO00560.

Protocols and materials databases

DNASU6386.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260130; ENSP00000260130; ENSG00000137575. [O00560-1]
ENST00000413219; ENSP00000411771; ENSG00000137575. [O00560-1]
ENST00000422546; ENSP00000391687; ENSG00000137575. [O00560-2]
ENST00000424270; ENSP00000395351; ENSG00000137575. [O00560-3]
ENST00000447182; ENSP00000409288; ENSG00000137575. [O00560-2]
GeneID6386.
KEGGhsa:6386.
UCSCuc003xtn.3. human. [O00560-1]
uc003xto.3. human. [O00560-2]
uc003xtp.3. human. [O00560-3]

Organism-specific databases

CTD6386.
GeneCardsGC08P059515.
HGNCHGNC:10662. SDCBP.
HPACAB012245.
HPA023840.
MIM602217. gene.
neXtProtNX_O00560.
PharmGKBPA35592.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG140434.
HOGENOMHOG000231604.
HOVERGENHBG053211.
InParanoidO00560.
KOK17254.
OrthoDBEOG75MVWZ.
PhylomeDBO00560.
TreeFamTF327131.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkO00560.

Gene expression databases

ArrayExpressO00560.
BgeeO00560.
CleanExHS_SDCBP.
GenevestigatorO00560.

Family and domain databases

Gene3D2.30.42.10. 2 hits.
InterProIPR001478. PDZ.
[Graphical view]
PfamPF00595. PDZ. 2 hits.
[Graphical view]
SMARTSM00228. PDZ. 2 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 2 hits.
PROSITEPS50106. PDZ. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSDCBP. human.
EvolutionaryTraceO00560.
GeneWikiSDCBP.
GenomeRNAi6386.
NextBio24796.
PROO00560.
SOURCESearch...

Entry information

Entry nameSDCB1_HUMAN
AccessionPrimary (citable) accession number: O00560
Secondary accession number(s): B2R5Q7 expand/collapse secondary AC list , B4DUH3, B7ZLN2, O00173, O43391, Q14CP2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM