Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q4ACU6 (SHAN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SH3 and multiple ankyrin repeat domains protein 3

Short name=Shank3
Alternative name(s):
Proline-rich synapse-associated protein 2
Short name=ProSAP2
SPANK-2
Gene names
Name:Shank3
Synonyms:Kiaa1650, Prosap2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1730 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major scaffold postsynaptic density protein which interacts with multiple proteins and complexes to orchestrate the dendritic spine and synapse formation, maturation and maintenance. Interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors via complexes with GKAP/PSD-95 and HOMER, respectively, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction through the interaction with Arp2/3 and WAVE1 complex as well as the promotion of the F-actin clusters. By way of this control of actin dynamics, participates in the regulation of developing neurons growth cone motility and the NMDA receptor-signaling. Also modulates GRIA1 exocytosis and GRM5/MGLUR5 expression and signaling to control the AMPA and metabotropic glutamate receptor-mediated synaptic transmission and plasticity. May be required at an early stage of synapse formation and be inhibited by IGF1 to promote synapse maturation. Ref.6 Ref.11 Ref.13 Ref.15

Subunit structure

May homomultimerize via its SAM domain. Interacts with BAIAP2, DBNL and SLC17A7/VGLUT1. Interacts with DLGAP1/GKAP, GRM1/MGLUR1, GRM5/MGLUR5 and LZTS3 C-termini via its PDZ domain. Interacts with ABI1, HOMER1, HOMER2, HOMER3 and CTTN/cortactin SH3 domain. Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts (via PDZ domain) with the GRIA1 subunit of the AMPA receptor (via PDZ-binding motif). Interacts with WASF1 and CYFIP2; the interactions mediate the association of SHANK3 with the WAVE1 complex. Interacts with ARPC2; the interaction probably mediates the association of SHANK3 with the Arp2/3 complex. Interacts (via ANK repeats) with SHARPIN and SPTAN1. Interacts (via PDZ domain) with ARHGAP44 (probably via PDZ-binding motif); the interaction takes place in dendritic spines and promotes GRIA1 exocytosis. Ref.2 Ref.6 Ref.13 Ref.15

Subcellular location

Cytoplasm. Cell junctionsynapse. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell projectiondendritic spine By similarity. Note: In neuronal cells, extends into the region subjacent to the postsynaptic density (PSD). Ref.2 Ref.3 Ref.15

Tissue specificity

In brain, highly expressed in striatum, thalamus, hippocampus and granule cells of the cerebellum. Ref.6 Ref.11 Ref.15

Developmental stage

Isoform 3 is weakly expressed at 17 dpc but its expression increases after birth. Ref.3

Domain

In isoform 1, the N-terminal region preceding the ANK repeats interacts with the 6 ANK repeats in an intramolecular manner, thereby restricting access to ligands, such as SHARPIN and SPTAN1 By similarity.

Disruption phenotype

Animals deficient for isoforms 1-7 exhibit self-injourious repetitive grooming and deficits in social interaction. They show defects at striatal synapses and cortico-striatal circuits with an increase in striatal volume, dendritic length, and surface area and a decrease of spine density, length and thickness of PSD. They seem to have an altered molecular composition of postsynaptic machinery in the striatum (Ref.11). In contrast, animals deficient for isoforms 1 and 2 exhibit a normal initiation of social interaction with a perturbed recognition of social novelty (Ref.11). In Ref.6, animals deficient for isoforms 1 and 2 show abnormal social behaviors, communication patterns, repetitive behaviors, learning and memory. In CA1 hippocampus, the synaptic plasticity is impaired with longer dendritic spines, decreased spine density and deficient long-term potentiation. The expression of specific synaptic scaffolding proteins and receptor subunits are altered. Animals deficient for isoforms 1-5 exhibit self-injourious repetitive grooming, brain-region-specific up-regulation of ionotropic glutamate receptors and increased levels of SHANK2 (Ref.12). Animals deficient for predominant isoforms containing exon 21 exhibit motor-coordination deficits, hypersensitivity to heat, novelty avoidance, altered locomotor response to novelty and minimal social abnormalities. They show a decrease in NMDA-AMPA excitatory postsynaptic current ratio in hippocampal CA1, reduced long-term potentiation and deficits in hippocampus-dependent spatial learning and memory (Ref.14). Ref.6 Ref.11 Ref.12 Ref.14

Sequence similarities

Belongs to the SHANK family.

Contains 6 ANK repeats.

Contains 1 PDZ (DHR) domain.

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   DomainANK repeat
Coiled coil
Repeat
SH3 domain
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from genetic interaction PubMed 15569713. Source: MGI

N-methyl-D-aspartate receptor clustering

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering

Inferred from mutant phenotype Ref.6PubMed 21795692. Source: BHF-UCL

brain morphogenesis

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

dendritic spine morphogenesis

Inferred from mutant phenotype PubMed 21167025Ref.11Ref.6. Source: BHF-UCL

embryonic epithelial tube formation

Inferred from genetic interaction PubMed 15569713. Source: MGI

guanylate kinase-associated protein clustering

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

learning

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

locomotory exploration behavior

Inferred from mutant phenotype Ref.11Ref.6. Source: BHF-UCL

memory

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

negative regulation of actin filament bundle assembly

Inferred from direct assay PubMed 19208628. Source: MGI

negative regulation of cell volume

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

neuromuscular process controlling balance

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

positive regulation of dendritic spine development

Inferred from mutant phenotype PubMed 21795692. Source: BHF-UCL

positive regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 21167025Ref.11PubMed 21795692. Source: BHF-UCL

positive regulation of glutamate receptor signaling pathway

Inferred from mutant phenotype PubMed 21795692. Source: BHF-UCL

positive regulation of long-term neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 21167025. Source: BHF-UCL

positive regulation of synapse structural plasticity

Inferred from mutant phenotype PubMed 21167025. Source: BHF-UCL

positive regulation of synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 21167025Ref.11PubMed 21795692. Source: BHF-UCL

postsynaptic density assembly

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

protein oligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of behavioral fear response

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

regulation of dendritic spine morphogenesis

Inferred from mutant phenotype PubMed 21795692. Source: BHF-UCL

regulation of grooming behavior

Inferred from mutant phenotype Ref.11Ref.6. Source: BHF-UCL

regulation of long term synaptic depression

Inferred from mutant phenotype PubMed 21795692. Source: BHF-UCL

regulation of long-term synaptic potentiation

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

social behavior

Inferred from mutant phenotype PubMed 21167025Ref.11Ref.6. Source: BHF-UCL

striatal medium spiny neuron differentiation

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

synapse assembly

Inferred from mutant phenotype Ref.11. Source: BHF-UCL

vocalization behavior

Inferred from mutant phenotype PubMed 21167025Ref.6. Source: BHF-UCL

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

ciliary membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendritic spine

Inferred from electronic annotation. Source: UniProtKB-SubCell

excitatory synapse

Inferred by curator Ref.11. Source: BHF-UCL

neuron projection

Inferred from direct assay PubMed 21795692. Source: BHF-UCL

neuron spine

Inferred from direct assay Ref.2. Source: BHF-UCL

neuronal postsynaptic density

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.2. Source: BHF-UCL

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionGKAP/Homer scaffold activity

Inferred from sequence or structural similarity. Source: BHF-UCL

SH3 domain binding

Inferred from sequence or structural similarity. Source: BHF-UCL

identical protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

ionotropic glutamate receptor binding

Inferred from physical interaction PubMed 15207857Ref.2. Source: BHF-UCL

protein C-terminus binding

Inferred from physical interaction Ref.2. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 15569713. Source: MGI

scaffold protein binding

Inferred from physical interaction Ref.2. Source: BHF-UCL

zinc ion binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 10 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Note: Additional isoform seem to exist. These isoforms may be the product of multiple intragenic promoter and/or alternative splicing.
Isoform 1 (identifier: Q4ACU6-1)

Also known as: A; 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.
Isoform 2 (identifier: Q4ACU6-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: MDGPGASAVV...NLDTPLPYLE → MGLCGSLLPTFSLSEQ
     703-710: Missing.
     784-790: EDEKLAS → SSAASVS
     791-1730: Missing.
Note: Produced by alternative promoter usage and alternative splicing.
Isoform 4 (identifier: Q4ACU6-3)

Also known as: C3; Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-433: MDGPGASAVV...SAGRGGHNKI → MEAPGAGFACPLPPGIASVTYVFVY
Note: Produced by alternative splicing of isoform 3.
Isoform 5 (identifier: Q4ACU6-6)

Also known as: C4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-433: MDGPGASAVV...SAGRGGHNKI → MEAPGAGFACPLPPGIASVTYVFVY
     784-790: EDEKLAS → SSAASVS
     791-1730: Missing.
Note: Produced by alternative splicing of isoform 3.
Isoform 6 (identifier: Q4ACU6-7)

Also known as: D1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-536: MDGPGASAVV...VQMRQYDTRH → MLPA
Note: Produced by alternative promoter usage.
Isoform 7 (identifier: Q4ACU6-8)

Also known as: D2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-589: MDGPGASAVV...GFGFVLRGAK → MLVNAFYLALPA
Note: Produced by alternative splicing of isoform 6.
Isoform 8 (identifier: Q4ACU6-9)

Also known as: E1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-675: MDGPGASAVV...KPEEDGARRR → MKKFASSRSL...RRAKASLFFA
Note: Produced by alternative promoter usage.
Isoform 9 (identifier: Q4ACU6-10)

Also known as: E2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-675: MDGPGASAVV...KPEEDGARRR → MKKFASSRSL...RRAKASLFFA
     703-710: Missing.
Note: Produced by alternative splicing of isoform 8.
Isoform 3 (identifier: Q4ACU6-11)

Also known as: C1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-528: Missing.
Note: Produced by alternative promoter usage.
Isoform 10 (identifier: Q4ACU6-12)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     1-890: Missing.
Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17301730SH3 and multiple ankyrin repeat domains protein 3
PRO_0000291257

Regions

Repeat148 – 17831ANK 1
Repeat182 – 21130ANK 2
Repeat215 – 24531ANK 3
Repeat249 – 27830ANK 4
Repeat282 – 31130ANK 5
Repeat315 – 34531ANK 6
Domain470 – 52960SH3
Domain570 – 66495PDZ
Domain1667 – 173064SAM
Region1 – 7575Intramolecular interaction with the ANK repeats By similarity
Region677 – 6848Required for interaction with ABI1 By similarity
Coiled coil1494 – 151421 Potential
Motif1410 – 14167SH3-binding Potential
Compositional bias435 – 46228Pro-rich
Compositional bias677 – 6804Poly-Pro
Compositional bias813 – 1349537Pro-rich

Amino acid modifications

Modified residue1221Phosphotyrosine Ref.9
Modified residue4821Phosphoserine Ref.7
Modified residue5551Phosphotyrosine Ref.9
Modified residue11591Phosphoserine By similarity
Modified residue11631Phosphoserine By similarity
Modified residue12341Phosphothreonine By similarity
Modified residue12531Phosphoserine By similarity
Modified residue16341Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 890890Missing in isoform 10.
VSP_053606
Alternative sequence1 – 675675MDGPG…GARRR → MKKFASSRSLNKILAQCDSS SREYEEVQAVERKWHLHLAT PRRLLLDRRAKASLFFA in isoform 8 and isoform 9.
VSP_053607
Alternative sequence1 – 589589MDGPG…LRGAK → MLVNAFYLALPA in isoform 7.
VSP_053608
Alternative sequence1 – 536536MDGPG…YDTRH → MLPA in isoform 6.
VSP_053609
Alternative sequence1 – 528528Missing in isoform 3.
VSP_053610
Alternative sequence1 – 433433MDGPG…GHNKI → MEAPGAGFACPLPPGIASVT YVFVY in isoform 4 and isoform 5.
VSP_053611
Alternative sequence1 – 8989MDGPG…LPYLE → MGLCGSLLPTFSLSEQ in isoform 2.
VSP_053612
Alternative sequence703 – 7108Missing in isoform 2 and isoform 9.
VSP_053613
Alternative sequence784 – 7907EDEKLAS → SSAASVS in isoform 2 and isoform 5.
VSP_053614
Alternative sequence791 – 1730940Missing in isoform 2 and isoform 5.
VSP_053615

Secondary structure

.................. 1730
Helix Strand Turn

Details...

Sequences

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

Last modified February 19, 2014. Version 3.
Checksum: 1343F857BE3EECD8

FASTA1,730185,397
        10         20         30         40         50         60 
MDGPGASAVV VRVGIPDLQQ TKCLRLDPTA PVWAAKQRVL CALNHSLQDA LNYGLFQPPS 

        70         80         90        100        110        120 
RGRAGKFLDE ERLLQDYPPN LDTPLPYLEF RYKRRVYAQN LIDDKQFAKL HTKANLKKFM 

       130        140        150        160        170        180 
DYVQLHSTDK VARLLDKGLD PNFHDPDSGE CPLSLAAQLD NATDLLKVLR NGGAHLDFRT 

       190        200        210        220        230        240 
RDGLTAVHCA TRQRNAGALT TLLDLGASPD YKDSRGLTPL YHSALGGGDA LCCELLLHDH 

       250        260        270        280        290        300 
AQLGTTDENG WQEIHQACRF GHVQHLEHLL FYGANMGAQN ASGNTALHIC ALYNQESCAR 

       310        320        330        340        350        360 
VLLFRGANKD VRNYNSQTAF QVAIIAGNFE LAEVIKTHKD SDVVPFRETP SYAKRRRLAG 

       370        380        390        400        410        420 
PSGLASPRPL QRSASDINLK GDQPAASPGP TLRSLPHQLL LQRLQEEKDR DRDGELENDI 

       430        440        450        460        470        480 
SGPSAGRGGH NKISPSGPGG SGPAPGPGPA SPAPPAPPPR GPKRKLYSAV PGRKFIAVKA 

       490        500        510        520        530        540 
HSPQGEGEIP LHRGEAVKVL SIGEGGFWEG TVKGRTGWFP ADCVEEVQMR QYDTRHETRE 

       550        560        570        580        590        600 
DRTKRLFRHY TVGSYDSLTS HSDYVIDDKV AILQKRDHEG FGFVLRGAKA ETPIEEFTPT 

       610        620        630        640        650        660 
PAFPALQYLE SVDVEGVAWR AGLRTGDFLI EVNGVNVVKV GHKQVVGLIR QGGNRLVMKV 

       670        680        690        700        710        720 
VSVTRKPEED GARRRAPPPP KRAPSTTLTL RSKSMTAELE ELASIRRRKG EKLDEILAVA 

       730        740        750        760        770        780 
AEPTLRPDIA DADSRAATVK QRPTSRRITP AEISSLFERQ GLPGPEKLPG SLRKGIPRTK 

       790        800        810        820        830        840 
SVGEDEKLAS LLEGRFPRST SMQDTVREGR GIPPPPQTAP PPPPAPYYFD SGPPPTFSPP 

       850        860        870        880        890        900 
PPPGRAYDTV RSSFKPGLEA RLGAGAAGLY DPSTPLGPLP YPERQKRARS MIILQDSAPE 

       910        920        930        940        950        960 
VGDVPRPAPA ATPPERPKRR PRPSGPDSPY ANLGAFSASL FAPSKPQRRK SPLVKQLQVE 

       970        980        990       1000       1010       1020 
DAQERAALAV GSPGPVGGSF AREPSPTHRG PRPGSLDYSS GEGLGLTFGG PSPGPVKERR 

      1030       1040       1050       1060       1070       1080 
LEERRRSTVF LSVGAIEGSP PSADLPSLQP SRSIDERLLG TGATTGRDLL LPSPVSALKP 

      1090       1100       1110       1120       1130       1140 
LVGGPSLGPS GSTFIHPLTG KPLDPSSPLA LALAARERAL ASQTPSRSPT PVHSPDADRP 

      1150       1160       1170       1180       1190       1200 
GPLFVDVQTR DSERGPLASP AFSPRSPAWI PVPARREAEK PPREERKSPE DKKSMILSVL 

      1210       1220       1230       1240       1250       1260 
DTSLQRPAGL IVVHATSNGQ EPSRLGAEEE RPGTPELAPA PMQAAAVAEP MPSPRAQPPG 

      1270       1280       1290       1300       1310       1320 
SIPADPGPGQ GSSEEEPELV FAVNLPPAQL SSSDEETREE LARIGLVPPP EEFANGILLT 

      1330       1340       1350       1360       1370       1380 
TPPPGPGPLP TTVPSPASGK PSSELPPAPE SAADSGVEEA DTRSSSDPHL ETTSTISTVS 

      1390       1400       1410       1420       1430       1440 
SMSTLSSESG ELTDTHTSFA DGHTFLLEKP PVPPKPKLKS PLGKGPVTFR DPLLKQSSDS 

      1450       1460       1470       1480       1490       1500 
ELMAQQHHAA STGLASAAGP ARPRYLFQRR SKLWGDPVES RGLPGPEDDK PTVISELSSR 

      1510       1520       1530       1540       1550       1560 
LQQLNKDTRS LGEEPVGGLG SLLDPAKKSP IAAARLFSSL GELSTISAQR SPGGPGGGAS 

      1570       1580       1590       1600       1610       1620 
YSVRPSGRYP VARRAPSPVK PASLERVEGL GAGVGGAGRP FGLTPPTILK SSSLSIPHEP 

      1630       1640       1650       1660       1670       1680 
KEVRFVVRSV SARSRSPSPS PLPSPSPGSG PSAGPRRPFQ QKPLQLWSKF DVGDWLESIH 

      1690       1700       1710       1720       1730 
LGEHRDRFED HEIEGAHLPA LTKEDFVELG VTRVGHRMNI ERALRQLDGS 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 5CF7C46C7DC4B486
Show »

FASTA70977,277
Isoform 4 (C3) (Beta) [UniParc].

Checksum: 4F90D15CB93B334C
Show »

FASTA1,322140,218
Isoform 5 (C4) [UniParc].

Checksum: 27B9B22AB57A32EE
Show »

FASTA38241,168
Isoform 6 (D1) [UniParc].

Checksum: FBDB744E8EC00FB4
Show »

FASTA1,198127,378
Isoform 7 (D2) [UniParc].

Checksum: C61D0CF8C4EE18F1
Show »

FASTA1,153122,073
Isoform 8 (E1) [UniParc].

Checksum: 749558749E5CCD1D
Show »

FASTA1,112118,003
Isoform 9 (E2) [UniParc].

Checksum: 1133661F14C1619A
Show »

FASTA1,104117,078
Isoform 3 (C1) [UniParc].

Checksum: D2247B82002EFA7E
Show »

FASTA1,202128,053
Isoform 10 (F) [UniParc].

Checksum: FD0680BF85041222
Show »

FASTA84088,196

References

« Hide 'large scale' references
[1]"Interaction of the Na+/Phosphate cotransporter type II with rSHANK."
Dehmelt L., Nalbant P., Werner A.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: C57B16/J.
Tissue: Kidney.
[2]"Direct interaction of post-synaptic density-95/Dlg/ZO-1 domain-containing synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor."
Uchino S., Wada H., Honda S., Nakamura Y., Ondo Y., Uchiyama T., Tsutsumi M., Suzuki E., Hirasawa T., Kohsaka S.
J. Neurochem. 97:1203-1214(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH GRIA1, SUBCELLULAR LOCATION.
[3]"Identification of two novel Shank3 transcripts in the developing mouse neocortex."
Waga C., Asano H., Sanagi T., Suzuki E., Nakamura Y., Tsuchiya A., Itoh M., Goto Y.I., Kohsaka S., Uchino S.
J. Neurochem. 128:280-293(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 875-1730.
Tissue: Brain.
[6]"Synaptic dysfunction and abnormal behaviors in mice lacking major isoforms of Shank3."
Wang X., McCoy P.A., Rodriguiz R.M., Pan Y., Je H.S., Roberts A.C., Kim C.J., Berrios J., Colvin J.S., Bousquet-Moore D., Lorenzo I., Wu G., Weinberg R.J., Ehlers M.D., Philpot B.D., Beaudet A.L., Wetsel W.C., Jiang Y.H.
Hum. Mol. Genet. 20:3093-3108(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 6; 7; 8 AND 9), ALTERNATIVE SPLICING, FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH HOMER1.
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1634, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-122 AND TYR-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[10]"Conserved role of intragenic DNA methylation in regulating alternative promoters."
Maunakea A.K., Nagarajan R.P., Bilenky M., Ballinger T.J., D'Souza C., Fouse S.D., Johnson B.E., Hong C., Nielsen C., Zhao Y., Turecki G., Delaney A., Varhol R., Thiessen N., Shchors K., Heine V.M., Rowitch D.H., Xing X. expand/collapse author list , Fiore C., Schillebeeckx M., Jones S.J., Haussler D., Marra M.A., Hirst M., Wang T., Costello J.F.
Nature 466:253-257(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE PROMOTER USAGE.
[11]"Shank3 mutant mice display autistic-like behaviours and striatal dysfunction."
Peca J., Feliciano C., Ting J.T., Wang W., Wells M.F., Venkatraman T.N., Lascola C.D., Fu Z., Feng G.
Nature 472:437-442(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[12]"Autistic-like behaviours and hyperactivity in mice lacking ProSAP1/Shank2."
Schmeisser M.J., Ey E., Wegener S., Bockmann J., Stempel A.V., Kuebler A., Janssen A.L., Udvardi P.T., Shiban E., Spilker C., Balschun D., Skryabin B.V., Dieck S.T., Smalla K.H., Montag D., Leblond C.S., Faure P., Torquet N. expand/collapse author list , Le Sourd A.M., Toro R., Grabrucker A.M., Shoichet S.A., Schmitz D., Kreutz M.R., Bourgeron T., Gundelfinger E.D., Boeckers T.M.
Nature 486:256-260(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[13]"Shank3-Rich2 interaction regulates AMPA receptor recycling and synaptic long-term potentiation."
Raynaud F., Janossy A., Dahl J., Bertaso F., Perroy J., Varrault A., Vidal M., Worley P.F., Boeckers T.M., Bockaert J., Marin P., Fagni L., Homburger V.
J. Neurosci. 33:9699-9715(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN AMPA RECEPTOR SIGNALING, INTERACTION WITH ARHGAP44.
[14]"Loss of predominant shank3 isoforms results in hippocampus-dependent impairments in behavior and synaptic transmission."
Kouser M., Speed H.E., Dewey C.M., Reimers J.M., Widman A.J., Gupta N., Liu S., Jaramillo T.C., Bangash M., Xiao B., Worley P.F., Powell C.M.
J. Neurosci. 33:18448-18468(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[15]"SHANK3 overexpression causes manic-like behaviour with unique pharmacogenetic properties."
Han K., Holder J.L. Jr., Schaaf C.P., Lu H., Chen H., Kang H., Tang J., Wu Z., Hao S., Cheung S.W., Yu P., Sun H., Breman A.M., Patel A., Lu H.C., Zoghbi H.Y.
Nature 503:72-77(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ACTIN-BINDING, INTERACTION WITH ARPC2; CYFIP2; DLG4; GKAP1; HOMER1 AND SLC17A7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ245904 mRNA. Translation: CAB89816.1.
AB841411 mRNA. Translation: BAN67189.1.
AB841412 mRNA. Translation: BAN67190.1.
AC122401 Genomic DNA. No translation available.
AC137513 Genomic DNA. No translation available.
AB231013 mRNA. Translation: BAE16756.1.
AK173228 mRNA. Translation: BAD32506.1.
HQ405757 mRNA. Translation: AEB77764.1.
HQ405758 mRNA. Translation: AEB77765.1.
HQ405759 mRNA. Translation: AEB77766.1.
HQ405760 mRNA. Translation: AEB77767.1.
HQ405761 mRNA. Translation: AEB77768.1.
HQ405762 mRNA. Translation: AEB77769.1.
HQ405763 mRNA. Translation: AEB77770.1.
RefSeqNP_067398.2. NM_021423.3. [Q4ACU6-1]
UniGeneMm.146855.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O5NX-ray1.83A/B/C/D/E/F/G/H562-669[»]
ProteinModelPortalQ4ACU6.
SMRQ4ACU6. Positions 562-667, 1664-1727.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208407. 4 interactions.
IntActQ4ACU6. 5 interactions.

PTM databases

PhosphoSiteQ4ACU6.

Proteomic databases

PaxDbQ4ACU6.
PRIDEQ4ACU6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000039074; ENSMUSP00000048062; ENSMUSG00000022623. [Q4ACU6-1]
ENSMUST00000066545; ENSMUSP00000064477; ENSMUSG00000022623. [Q4ACU6-2]
GeneID58234.
KEGGmmu:58234.
UCSCuc007xha.2. mouse. [Q4ACU6-1]
uc007xhb.2. mouse.

Organism-specific databases

CTD85358.
MGIMGI:1930016. Shank3.
RougeSearch...

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00510000046474.
HOGENOMHOG000293276.
HOVERGENHBG054027.
InParanoidQ4ACU6.
KOK15009.
OrthoDBEOG7GBFW2.
PhylomeDBQ4ACU6.
TreeFamTF324593.

Gene expression databases

ArrayExpressQ4ACU6.
BgeeQ4ACU6.
CleanExMM_SHANK3.
GenevestigatorQ4ACU6.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
1.25.40.20. 1 hit.
2.30.42.10. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF12796. Ank_2. 2 hits.
PF00595. PDZ. 1 hit.
PF00536. SAM_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 5 hits.
SM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS50106. PDZ. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSHANK3. mouse.
EvolutionaryTraceQ4ACU6.
NextBio314265.
PROQ4ACU6.
SOURCESearch...

Entry information

Entry nameSHAN3_MOUSE
AccessionPrimary (citable) accession number: Q4ACU6
Secondary accession number(s): F8S0X0 expand/collapse secondary AC list , F8S0X2, F8S0X3, F8S0X5, F8S0X6, Q69ZD8, Q9JJZ3, S6BMD3, S6CCV8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: February 19, 2014
Last modified: July 9, 2014
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot