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Protein

Syntenin-2

Gene

SDCBP2

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

Functioni

Binds phosphatidylinositol 4,5-bisphosphate (PIP2). May play a role in the organization of nuclear PIP2, cell division and cell survival (PubMed:15961997).1 Publication

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: UniProtKB
  • intracellular signal transduction Source: UniProtKB
  • intracellular transport Source: UniProtKB
  • nervous system development Source: UniProtKB

Keywordsi

LigandLipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Syntenin-2
Alternative name(s):
Similar to TACIP181 Publication
Short name:
SITAC1 Publication
Syndecan-binding protein 2
Gene namesi
Name:SDCBP2Imported
Synonyms:SITAC18
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000125775.14.
HGNCiHGNC:15756. SDCBP2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi113K → A: Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-167; A-197 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-167. 1 Publication1
Mutagenesisi167K → A: Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-197 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-113. 1 Publication1
Mutagenesisi197K → A: Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-167 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-244. 1 Publication1
Mutagenesisi244K → A: Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-167 and A-197. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-197. 1 Publication1

Organism-specific databases

DisGeNETi27111.
OpenTargetsiENSG00000125775.
PharmGKBiPA38033.

Polymorphism and mutation databases

BioMutaiSDCBP2.
DMDMi20455288.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001840041 – 292Syntenin-2Add BLAST292

Proteomic databases

EPDiQ9H190.
MaxQBiQ9H190.
PaxDbiQ9H190.
PeptideAtlasiQ9H190.
PRIDEiQ9H190.

PTM databases

iPTMnetiQ9H190.
PhosphoSitePlusiQ9H190.
SwissPalmiQ9H190.

Expressioni

Tissue specificityi

Preferentially expressed in cells of the digestive tract (PubMed:11102519). Low expression in skeletal muscle and kidney (PubMed:11102519). Detected in differentiated keratinocytes of normal and malignant epithelium (PubMed:22623796). In healthy skin, expression is localized in suprabasal epidermal layers (PubMed:22623796).2 Publications

Inductioni

Down-regulated by HPV8 E6 papillomavirus (HPV) oncoprotein (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000125775.
CleanExiHS_SDCBP2.
GenevisibleiQ9H190. HS.

Organism-specific databases

HPAiHPA054554.

Interactioni

Subunit structurei

Monomer and homodimer (PubMed:11152476, PubMed:23300061). Interacts with SDCBP (PubMed:11152476). Interacts with TM4SF1 (PubMed:11102519).3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi118007. 39 interactors.
IntActiQ9H190. 66 interactors.
MINTiMINT-1438328.

Structurei

3D structure databases

ProteinModelPortaliQ9H190.
SMRiQ9H190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini108 – 187PDZ 1PROSITE-ProRule annotationAdd BLAST80
Domaini192 – 267PDZ 2PROSITE-ProRule annotationAdd BLAST76

Domaini

Binds phosphatidylinositol 4,5-bisphosphate (PIP2) via its two PDZ domains. These domains target SDCBP2 to the plasma membranes and nucleoli, two PIP2-rich regions.1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IK98. Eukaryota.
ENOG410YNPQ. LUCA.
GeneTreeiENSGT00390000014465.
HOGENOMiHOG000231604.
HOVERGENiHBG053211.
InParanoidiQ9H190.
OMAiEIHLCKD.
OrthoDBiEOG091G0HJI.
PhylomeDBiQ9H190.
TreeFamiTF327131.

Family and domain databases

InterProiView protein in InterPro
IPR001478. PDZ.
IPR036034. PDZ_sf.
PfamiView protein in Pfam
PF00595. PDZ. 1 hit.
SMARTiView protein in SMART
SM00228. PDZ. 2 hits.
SUPFAMiSSF50156. SSF50156. 2 hits.
PROSITEiView protein in PROSITE
PS50106. PDZ. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H190-1) [UniParc]FASTAAdd to basket
Also known as: Alpha

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
MSSLYPSLED LKVDQAIQAQ VRASPKMPAL PVQATAISPP PVLYPNLAEL
60 70 80 90 100
ENYMGLSLSS QEVQESLLQI PEGDSTAVSG PGPGQMVAPV TGYSLGVRRA
110 120 130 140 150
EIKPGVREIH LCKDERGKTG LRLRKVDQGL FVQLVQANTP ASLVGLRFGD
160 170 180 190 200
QLLQIDGRDC AGWSSHKAHQ VVKKASGDKI VVVVRDRPFQ RTVTMHKDSM
210 220 230 240 250
GHVGFVIKKG KIVSLVKGSS AARNGLLTNH YVCEVDGQNV IGLKDKKIME
260 270 280 290
ILATAGNVVT LTIIPSVIYE HMVKKLPPVL LHHTMDHSIP DA
Length:292
Mass (Da):31,594
Last modified:May 2, 2002 - v2
Checksum:iE12536839E1CD91C
GO
Isoform 3 (identifier: Q9H190-3) [UniParc]FASTAAdd to basket
Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Show »
Length:207
Mass (Da):22,664
Checksum:i16913A0148BF691A
GO

Sequence cautioni

Q9H190: The sequence AAH02727 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69Q → H in CAC21716 (PubMed:11152476).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_053700182V → M2 PublicationsCorresponds to variant dbSNP:rs2273959Ensembl.1
Natural variantiVAR_036544191R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs35367003Ensembl.1
Natural variantiVAR_053701223R → C. Corresponds to variant dbSNP:rs1048621Ensembl.1
Natural variantiVAR_053702242G → R. Corresponds to variant dbSNP:rs4814111Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0063521 – 85Missing in isoform 3. 2 PublicationsAdd BLAST85

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159228 mRNA. Translation: AAF80369.1.
AJ292245 mRNA. Translation: CAC21573.1.
AJ292244 mRNA. Translation: CAC21716.1.
AF131809 mRNA. Translation: AAD20049.1.
AL136531 Genomic DNA. Translation: CAC16178.1.
AL136531 Genomic DNA. Translation: CAH72383.1.
BC002727 mRNA. Translation: AAH02727.2. Different initiation.
CCDSiCCDS13013.1. [Q9H190-3]
CCDS42848.1. [Q9H190-1]
RefSeqiNP_001186713.1. NM_001199784.1. [Q9H190-1]
NP_056500.2. NM_015685.5. [Q9H190-3]
NP_536737.3. NM_080489.4. [Q9H190-1]
UniGeneiHs.657015.

Genome annotation databases

EnsembliENST00000339987; ENSP00000342935; ENSG00000125775. [Q9H190-1]
ENST00000360779; ENSP00000354013; ENSG00000125775. [Q9H190-1]
ENST00000381808; ENSP00000371229; ENSG00000125775. [Q9H190-3]
ENST00000381812; ENSP00000371233; ENSG00000125775. [Q9H190-1]
GeneIDi27111.
KEGGihsa:27111.
UCSCiuc002weu.5. human. [Q9H190-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSDCB2_HUMAN
AccessioniPrimary (citable) accession number: Q9H190
Secondary accession number(s): O95892
, Q5W0X1, Q9BZ42, Q9H567, Q9NRY8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 2, 2002
Last modified: October 25, 2017
This is version 143 of the entry and version 2 of the sequence. See 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

Caution

The nuclear speckles location of SDCBP2 is under debate. One study shows that in paraformaldehyde fixed cells, SDCBP2 is highly enriched in nuclear speckles (PubMed:15961997). The same authors investigate subcellular location in living cells and fail to detect SDCBP2 in nuclear speckles, and propose that enrichment in nuclear speckles is fixation-dependent (PubMed:23300061).2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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