O00560 (SDCB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SDCBP
Synonyms:	MDA9, SYCL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 junction › focal adhesion. Cell junction › adherens junction. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Nucleus. Melanosome. Cytoplasm › cytosol. Cytoplasm › cytoskeleton. 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 component	Cell junction Cell membrane Cytoplasm Cytoskeleton Endoplasmic reticulum Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Ras protein signal transduction Inferred from electronic annotation. Source: Compara 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_component	adherens junction Non-traceable author statement Ref.14. Source: UniProtKB 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 nucleus Non-traceable author statement Ref.14. Source: UniProtKB
Molecular_function	cytoskeletal adaptor activity Non-traceable author statement Ref.2. Source: UniProtKB interleukin-5 receptor binding Inferred from sequence or structural similarity Ref.15. Source: UniProtKB syndecan binding Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 298

297

Syntenin-1

PRO_0000184001

Regions

Domain

114 – 193

80

PDZ 1

Domain

198 – 273

76

PDZ 2

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.9

Natural variations

Alternative sequence

12 – 17

6

Missing in isoform 3.

VSP_038374

Alternative sequence

81

1

Missing in isoform 2.

VSP_038375

Natural variant

26

1

P → T.
Corresponds to variant rs11550282 [ dbSNP | Ensembl ].

VAR_053699

Natural variant

69

1

N → S. Ref.2
Corresponds to variant rs1127509 [ dbSNP | Ensembl ].

VAR_013160

Experimental info

Sequence conflict

62

1

N → S in AAB51246. Ref.2

Secondary structure

1

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298

Helix Strand Turn

Details...

Beta strand

113 – 118

6

Beta strand

121 – 123

3

Beta strand

126 – 132

7

Beta strand

135 – 141

7

Helix

146 – 149

4

Beta strand

157 – 161

5

Helix

171 – 180

10

Beta strand

183 – 191

9

Beta strand

197 – 202

6

Beta strand

205 – 208

4

Beta strand

211 – 214

4

Beta strand

217 – 221

5

Helix

226 – 230

5

Beta strand

234 – 241

8

Helix

251 – 260

10

Beta strand

263 – 271

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 574E1349F86F949F	FASTA	298	32,444
	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
	Isoform 2 [UniParc]. Checksum: 67FED210EFB6EEF6	FASTA	297	32,316
	10 20 30 40 50 60 MSLYPSLEDL KVDKVIQAQT AFSANPANPA ILSEASAPIP HDGNLYPRLY PELSQYMGLS 70 80 90 100 110 120 LNEEEIRANV AVVSGAPLQG LVARPSSINY MVAPVTGNDV GIRRAEIKQG IREVILCKDQ 130 140 150 160 170 180 DGKIGLRLKS IDNGIFVQLV QANSPASLVG LRFGDQVLQI NGENCAGWSS DKAHKVLKQA 190 200 210 220 230 240 FGEKITMTIR DRPFERTITM HKDSTGHVGF IFKNGKITSI VKDSSAARNG LLTEHNICEI 250 260 270 280 290 NGQNVIGLKD SQIADILSTS GTVVTITIMP AFIFEHIIKR MAPSIMKSLM DHTIPEV
	Isoform 3 [UniParc]. Checksum: 004BFE46AC4D9FBA	FASTA	292	31,762
	10 20 30 40 50 60 MSLYPSLEDL KAQTAFSANP ANPAILSEAS APIPHDGNLY PRLYPELSQY MGLSLNEEEI 70 80 90 100 110 120 RANVAVVSGA PLQGQLVARP SSINYMVAPV TGNDVGIRRA EIKQGIREVI LCKDQDGKIG 130 140 150 160 170 180 LRLKSIDNGI FVQLVQANSP ASLVGLRFGD QVLQINGENC AGWSSDKAHK VLKQAFGEKI 190 200 210 220 230 240 TMTIRDRPFE RTITMHKDST GHVGFIFKNG KITSIVKDSS AARNGLLTEH NICEINGQNV 250 260 270 280 290 IGLKDSQIAD ILSTSGTVVT ITIMPAFIFE HIIKRMAPSI MKSLMDHTIP EV

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, 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], MASS SPECTROMETRY. 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], MASS SPECTROMETRY. Tissue: Melanoma.
[18]	"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].
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.

IPI

IPI00299086.
IPI00478874.
IPI00479018.

PIR

JC6537.

RefSeq

NP_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.

UniGene

Hs.200804.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O00560.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42705N.

IntAct

O00560. 46 interactions.

MINT

MINT-5002159.

STRING

9606.ENSP00000260130.

PTM databases

PhosphoSite

O00560.

Proteomic databases

PaxDb

O00560.

PRIDE

O00560.

Protocols and materials databases

DNASU

6386.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260130; ENSP00000260130; ENSG00000137575.
ENST00000413219; ENSP00000411771; ENSG00000137575.
ENST00000422546; ENSP00000391687; ENSG00000137575.
ENST00000424270; ENSP00000395351; ENSG00000137575.
ENST00000447182; ENSP00000409288; ENSG00000137575.

GeneID

6386.

KEGG

hsa:6386.

UCSC

uc003xtn.3. human.
uc003xto.3. human.
uc003xtp.3. human.

Organism-specific databases

CTD

6386.

GeneCards

GC08P059515.

HGNC

HGNC:10662. SDCBP.

HPA

CAB012245.
HPA023840.

MIM

602217. gene.

neXtProt

NX_O00560.

PharmGKB

PA35592.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG140434.

HOGENOM

HOG000231604.

HOVERGEN

HBG053211.

InParanoid

O00560.

OrthoDB

EOG47WNPB.

PhylomeDB

O00560.

Enzyme and pathway databases

Pathway_Interaction_DB

syndecan_1_pathway. Syndecan-1-mediated signaling events.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

O00560.

Bgee

O00560.

CleanEx

HS_SDCBP.

Genevestigator

O00560.

GermOnline

ENSG00000137575. Homo sapiens.

Family and domain databases

InterPro

IPR001478. PDZ.
[Graphical view]

Pfam

PF00595. PDZ. 2 hits.
[Graphical view]

SMART

SM00228. PDZ. 2 hits.
[Graphical view]

SUPFAM

SSF50156. PDZ. 2 hits.

PROSITE

PS50106. PDZ. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SDCBP. human.

EvolutionaryTrace

O00560.

GenomeRNAi

6386.

NextBio

24796.

SOURCE

Search...

Entry information

Entry name

SDCB1_HUMAN

Accession

Primary (citable) accession number: O00560
Secondary accession number(s): B2R5Q7 , B4DUH3, B7ZLN2, O00173, O43391, Q14CP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.