Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

SH3 and multiple ankyrin repeat domains protein 3

Gene

Shank3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  • GKAP/Homer scaffold activity Source: BHF-UCL
  • identical protein binding Source: IntAct
  • ionotropic glutamate receptor binding Source: BHF-UCL
  • protein C-terminus binding Source: BHF-UCL
  • protein self-association Source: RGD
  • scaffold protein binding Source: BHF-UCL
  • SH3 domain binding Source: RGD
  • zinc ion binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Shank3
Synonyms:Prosap2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69264. Shank3.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • ciliary membrane Source: BHF-UCL
  • cytoplasm Source: UniProtKB-SubCell
  • dendritic spine Source: UniProtKB-SubCell
  • neuronal postsynaptic density Source: BHF-UCL
  • neuron projection Source: BHF-UCL
  • neuron spine Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • postsynaptic density Source: UniProtKB
  • postsynaptic membrane Source: UniProtKB-KW
  • synapse Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121R → C: Disrupts postsynaptic AMPA and NMDA receptor-mediated synaptic transmission as well as transsynaptic signaling and spine maturation. 2 Publications
Mutagenesisi68 – 681L → P: Slightly increases interaction with SHARPIN and SPTAN1. No effect on localization. 1 Publication
Mutagenesisi300 – 3001R → C: Disrupts postsynaptic AMPA and NMDA receptor-mediated synaptic transmission as well as transsynaptic signaling and spine maturation. Slightly decreases interaction with SHARPIN and SPTAN1. No effect on localization. 3 Publications
Mutagenesisi321 – 3211Q → R: Disrupts postsynaptic AMPA and NMDA receptor-mediated synaptic transmission as well as transsynaptic signaling and spine maturation. Disrupts axonal growth cone motility. Slightly increases interaction with SHARPIN and SPTAN1. No effect on localization. 3 Publications
Mutagenesisi677 – 6771P → A: Strongly decreases interaction with ABI1. 1 Publication
Mutagenesisi678 – 6781P → A: Almost abolishes interaction with ABI1. 1 Publication
Mutagenesisi679 – 6791P → A: Abolishes interaction with ABI1. 1 Publication
Mutagenesisi680 – 6801P → A: Abolishes interaction with ABI1. 1 Publication
Mutagenesisi684 – 6841P → A: Abolishes interaction with ABI1. 1 Publication
Mutagenesisi1311 – 13111P → L: Abolishes interaction with HOMER1 isoform 3. 1 Publication
Mutagenesisi1314 – 13141F → C: Abolishes interaction with HOMER1 isoform 3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17401740SH3 and multiple ankyrin repeat domains protein 3PRO_0000174676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei122 – 1221PhosphotyrosineBy similarity
Modified residuei373 – 3731PhosphoserineBy similarity
Modified residuei375 – 3751PhosphoserineCombined sources
Modified residuei387 – 3871PhosphoserineCombined sources
Modified residuei394 – 3941PhosphoserineCombined sources
Modified residuei482 – 4821PhosphoserineBy similarity
Modified residuei555 – 5551PhosphotyrosineBy similarity
Modified residuei694 – 6941PhosphoserineBy similarity
Modified residuei781 – 7811PhosphoserineBy similarity
Modified residuei790 – 7901PhosphoserineBy similarity
Modified residuei801 – 8011PhosphoserineBy similarity
Modified residuei891 – 8911PhosphoserineBy similarity
Modified residuei898 – 8981PhosphoserineBy similarity
Modified residuei913 – 9131PhosphothreonineBy similarity
Modified residuei931 – 9311PhosphotyrosineCombined sources
Modified residuei1131 – 11311PhosphothreonineCombined sources
Modified residuei1135 – 11351PhosphoserineCombined sources
Modified residuei1160 – 11601PhosphoserineCombined sources
Modified residuei1164 – 11641PhosphoserineBy similarity
Modified residuei1167 – 11671PhosphoserineCombined sources
Modified residuei1235 – 12351PhosphothreonineCombined sources
Modified residuei1254 – 12541PhosphoserineCombined sources
Modified residuei1421 – 14211PhosphoserineCombined sources
Modified residuei1511 – 15111PhosphoserineCombined sources
Modified residuei1522 – 15221PhosphoserineBy similarity
Modified residuei1530 – 15301PhosphoserineBy similarity
Modified residuei1549 – 15491PhosphoserineBy similarity
Modified residuei1644 – 16441PhosphoserineCombined sources
Modified residuei1646 – 16461PhosphoserineBy similarity
Modified residuei1648 – 16481PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9JLU4.
PRIDEiQ9JLU4.

PTM databases

iPTMnetiQ9JLU4.
PhosphoSiteiQ9JLU4.

Expressioni

Tissue specificityi

Widely expressed in brain (at protein level).5 Publications

Interactioni

Subunit structurei

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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-6271152,EBI-6271152
Abi1Q9QZM57EBI-6271152,EBI-920097
Arhgef7Q9ES28-22EBI-6271152,EBI-8620514From a different organism.

GO - Molecular functioni

  • GKAP/Homer scaffold activity Source: BHF-UCL
  • identical protein binding Source: IntAct
  • ionotropic glutamate receptor binding Source: BHF-UCL
  • protein C-terminus binding Source: BHF-UCL
  • protein self-association Source: RGD
  • scaffold protein binding Source: BHF-UCL
  • SH3 domain binding Source: RGD

Protein-protein interaction databases

BioGridi248756. 9 interactions.
IntActiQ9JLU4. 8 interactions.
MINTiMINT-1486849.
STRINGi10116.ENSRNOP00000041083.

Structurei

Secondary structure

1
1740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1674 – 16763Combined sources
Helixi1679 – 168810Combined sources
Helixi1692 – 16943Combined sources
Helixi1695 – 17006Combined sources
Helixi1705 – 17106Combined sources
Helixi1713 – 17186Combined sources
Helixi1724 – 173512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F3NX-ray2.10A/B/C1674-1740[»]
2F44X-ray2.40A/B/C1674-1740[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLU4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati148 – 18134ANK 1Add
BLAST
Repeati182 – 21433ANK 2Add
BLAST
Repeati215 – 24531ANK 3Add
BLAST
Repeati249 – 27830ANK 4Add
BLAST
Repeati282 – 31130ANK 5Add
BLAST
Repeati315 – 34531ANK 6Add
BLAST
Domaini470 – 52960SH3PROSITE-ProRule annotationAdd
BLAST
Domaini570 – 66495PDZPROSITE-ProRule annotationAdd
BLAST
Domaini1677 – 174064SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7575Intramolecular interaction with the ANK repeatsAdd
BLAST
Regioni677 – 6848Required for interaction with ABI1

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1495 – 151521Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1411 – 14177SH3-bindingSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi820 – 8267Poly-Pro
Compositional biasi839 – 8446Poly-Pro

Domaini

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 SPTAN1.1 Publication

Sequence similaritiesi

Belongs to the SHANK family.Curated
Contains 6 ANK repeats.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4375. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000293276.
HOVERGENiHBG054027.
InParanoidiQ9JLU4.
KOiK15009.
OrthoDBiEOG7GBFW2.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR032425. FERM_f0.
IPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF16511. FERM_f0. 1 hit.
PF00536. SAM_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 5 hits.
SM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50297. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. These isoforms may be the product of multiple intragenic promoter and/or alternative splicing.

Isoform 2 (identifier: Q9JLU4-1) [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
MDGPGASAVV VRVGIPDLQQ TKCLRLDPTA PVWAAKQRVL CALNHSLQDA
60 70 80 90 100
LNYGLFQPPS RGRAGKFLDE ERLLQDYPPN LDTPLPYLEF RYKRRVYAQN
110 120 130 140 150
LIDDKQFAKL HTKANLKKFM DYVQLHSTDK VARLLDKGLD PNFHDPDSGE
160 170 180 190 200
CPLSLAAQLD NATDLLKVLR NGGAHLDFRT RDGLTAVHCA TRQRNAGALT
210 220 230 240 250
TLLDLGASPD YKDSRGLTPL YHSALGGGDA LCCELLLHDH AQLGTTDENG
260 270 280 290 300
WQEIHQACRF GHVQHLEHLL FYGANMGAQN ASGNTALHIC ALYNQESCAR
310 320 330 340 350
VLLFRGANKD VRNYNSQTAF QVAIIAGNFE LAEVIKTHKD SDVVPFRETP
360 370 380 390 400
SYAKRRRLAG PSGLASPRPL QRSASDINLK GDQPAASPGP TLRSLPHQLL
410 420 430 440 450
LQRLQEEKDR DRDGEQENDI SGPSAGRGGH SKISPSGPGG SGPAPGPGPA
460 470 480 490 500
SPAPPAPPPR GPKRKLYSAV PGRKFIAVKA HSPQGEGEIP LHRGEAVKVL
510 520 530 540 550
SIGEGGFWEG TVKGRTGWFP ADCVEEVQMR QYDTRHETRE DRTKRLFRHY
560 570 580 590 600
TVGSYDSLTS HSDYVIDDKV AILQKRDHEG FGFVLRGAKA ETPIEEFTPT
610 620 630 640 650
PAFPALQYLE SVDVEGVAWK AGLRTGDFLI EVNGVNVVKV GHKQVVGLIR
660 670 680 690 700
QGGNRLVMKV VSVTRKPEED SARRRAPPPP KRAPSTTLTL RSKSMTAELE
710 720 730 740 750
ELASIRRRKG EKLDEILAVA AEPTLRPDIA DADSRAATVK QRPTSRRITP
760 770 780 790 800
AEISSLFERQ GLPGPEKLPG SLRKGIPRTK SVGEDEKLAS LLEGRFPRST
810 820 830 840 850
SMQDTVREGR GIPPPPQTAP PPPPAPYYFD SGPPPTFSPP PPPPGRAYDT
860 870 880 890 900
VRSSFKPGLE ARLGAGAAGL YDSGTPLGPL PYPERQKRAR SMIILQDSAP
910 920 930 940 950
EVGDVPRPAP AATPPERPKR RPRPSGPDSP YANLGAFSAS LFAPSKPQRR
960 970 980 990 1000
KSPLVKQLQV EDAQERAALA VGSPGPVGGS FAREPSPTHR GPRPGGLDYS
1010 1020 1030 1040 1050
SGEGLGLTFG GPSPGPVKER RLEERRRSTV FLSVGAIEGS PPSADLPSLQ
1060 1070 1080 1090 1100
PSRSIDERLL GTGATTGRDL LLPSPVSALK PLVGGPSLGP SGSTFIHPLT
1110 1120 1130 1140 1150
GKPLDPSSPL ALALAARERA LASQTPSRSP TPVHSPDADR PGPLFVDVQT
1160 1170 1180 1190 1200
RDSERGPLAS PAFSPRSPAW IPVPARREAE KPTREERKSP EDKKSMILSV
1210 1220 1230 1240 1250
LDTSLQRPAG LIVVHATSNG QEPNRLGAEE ERPGTPELAP TPMQAAAVAE
1260 1270 1280 1290 1300
PMPSPRAQPP GSIPADPGPG QGSSEEEPEL VFAVNLPPAQ LSSSDEETRE
1310 1320 1330 1340 1350
ELARIGLVPP PEEFANGILL ATPPPGPGPL PTTVPSPASG KPSSELPPAP
1360 1370 1380 1390 1400
ESAADSGVEE ADTRSSSDPH LETTSTISTV SSMSTLSSES GELTDTHTSF
1410 1420 1430 1440 1450
ADGHTFLLEK PPVPPKPKLK SPLGKGPVTF RDPLLKQSSD SELMAQQHHA
1460 1470 1480 1490 1500
TSTGLTSAAG PARPRYLFQR RSKLWGDPVE SRGLPGPEDD KPTVISELSS
1510 1520 1530 1540 1550
RLQQLNKDTR SLGEEPVGGL GSLLDPAKKS PIAAARCAVV PSAGWLFSSL
1560 1570 1580 1590 1600
GELSTISAQR SPGGPGGGAS YSVRPSGRYP VARRAPSPVK PASLERVEGL
1610 1620 1630 1640 1650
GAGVGGAGRP FGLTPPTILK SSSLSIPHEP KEVRFVVRSV SARSRSPSPS
1660 1670 1680 1690 1700
PLPSPSPGSG PSAGPRRPFQ QKPLQLWSKF DVGDWLESIH LGEHRDRFED
1710 1720 1730 1740
HEIEGAHLPA LTKEDFVELG VTRVGHRMNI ERALRQLDGS
Length:1,740
Mass (Da):186,376
Last modified:February 19, 2014 - v3
Checksum:iA9F486E893EA5AA0
GO
Isoform 1 (identifier: Q9JLU4-2) [UniParc]FASTAAdd to basket

Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     1537-1545: Missing.

Show »
Length:1,731
Mass (Da):185,505
Checksum:i1EFFF01A410FEACE
GO
Isoform 3 (identifier: Q9JLU4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1129-1136: SPTPVHSP → PRRRAGMV
     1137-1740: Missing.

Show »
Length:1,136
Mass (Da):122,694
Checksum:i5867719D77B65948
GO

Sequence cautioni

The sequence AAD42976.1 differs from that shown. Reason: Frameshift at positions 898 and 925. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971H → L in AAD42976 (PubMed:10958799).Curated
Sequence conflicti706 – 7061R → G in AAD42976 (PubMed:10958799).Curated
Sequence conflicti827 – 8326YYFDSG → ILRLR in AAD42976 (PubMed:10958799).Curated
Sequence conflicti837 – 8426FSPPPP → SHHGHQ in AAD42976 (PubMed:10958799).Curated
Sequence conflicti846 – 8461R → G in AAD42976 (PubMed:10958799).Curated
Sequence conflicti888 – 8881R → G in AAD42976 (PubMed:10958799).Curated
Sequence conflicti1040 – 10401S → N in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1087 – 10871S → N in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1092 – 10921G → S in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1262 – 12621S → N in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1270 – 12701G → S in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1273 – 12731S → N in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1279 – 12791E → K in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1294 – 12941S → N in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1432 – 14321D → G in AAF61375 (PubMed:10433268).Curated
Sequence conflicti1640 – 16401V → A in AAF61375 (PubMed:10433268).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1129 – 11368SPTPVHSP → PRRRAGMV in isoform 3. CuratedVSP_006087
Alternative sequencei1137 – 1740604Missing in isoform 3. CuratedVSP_006088Add
BLAST
Alternative sequencei1537 – 15459Missing in isoform 1. 2 PublicationsVSP_006089

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF133301 mRNA. Translation: AAF61375.1.
AJ133120 mRNA. Translation: CAB45688.1.
AF159047 mRNA. Translation: AAD42976.1. Frameshift.
RefSeqiNP_067708.1. NM_021676.1.
UniGeneiRn.42876.

Genome annotation databases

GeneIDi59312.
KEGGirno:59312.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF133301 mRNA. Translation: AAF61375.1.
AJ133120 mRNA. Translation: CAB45688.1.
AF159047 mRNA. Translation: AAD42976.1. Frameshift.
RefSeqiNP_067708.1. NM_021676.1.
UniGeneiRn.42876.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F3NX-ray2.10A/B/C1674-1740[»]
2F44X-ray2.40A/B/C1674-1740[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248756. 9 interactions.
IntActiQ9JLU4. 8 interactions.
MINTiMINT-1486849.
STRINGi10116.ENSRNOP00000041083.

PTM databases

iPTMnetiQ9JLU4.
PhosphoSiteiQ9JLU4.

Proteomic databases

PaxDbiQ9JLU4.
PRIDEiQ9JLU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi59312.
KEGGirno:59312.

Organism-specific databases

CTDi85358.
RGDi69264. Shank3.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4375. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000293276.
HOVERGENiHBG054027.
InParanoidiQ9JLU4.
KOiK15009.
OrthoDBiEOG7GBFW2.

Miscellaneous databases

EvolutionaryTraceiQ9JLU4.
NextBioi611861.
PROiQ9JLU4.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.20. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR032425. FERM_f0.
IPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF16511. FERM_f0. 1 hit.
PF00536. SAM_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 5 hits.
SM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50297. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family."
    Boeckers T.M., Winter C., Smalla K.-H., Kreutz M.R., Bockmann J., Seidenbecher C., Garner C.C., Gundelfinger E.D.
    Biochem. Biophys. Res. Commun. 264:247-252(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DLGAP1 AND DLG4, TISSUE SPECIFICITY.
  2. "Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin."
    Naisbitt S., Kim E., Tu J.C., Xiao B., Sala C., Valtschanoff J., Weinberg R.J., Worley P.F., Sheng M.
    Neuron 23:569-582(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DLGAP1 AND CTTN, OLIGOMERIZATION.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  3. "The G protein-coupled receptor CL1 interacts directly with proteins of the Shank family."
    Tobaben S., Suedhof T.C., Stahl B.
    J. Biol. Chem. 275:36204-36210(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. "Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of postsynaptic density proteins."
    Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P., Doan A., Aakalu V.K., Lanahan A.A., Sheng M., Worley P.F.
    Neuron 23:583-592(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOMER1; HOMER2; HOMER3; DLGAP1; MGLUR1A AND MGLUR5, MUTAGENESIS OF PRO-1311 AND PHE-1314.
  5. "The Shank family of scaffold proteins."
    Sheng M., Kim E.
    J. Cell Sci. 113:1851-1856(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  6. "Linkage of the actin cytoskeleton to the postsynaptic density via direct interactions of Abp1 with the ProSAP/Shank family."
    Qualmann B., Boeckers T.M., Jeromin M., Gundelfinger E.D., Kessels M.M.
    J. Neurosci. 24:2481-2495(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DBNL, TISSUE SPECIFICITY.
  7. "ProSAP-interacting protein 1 (ProSAPiP1), a novel protein of the postsynaptic density that links the spine-associated Rap-Gap (SPAR) to the scaffolding protein ProSAP2/Shank3."
    Wendholt D., Spilker C., Schmitt A., Dolnik A., Smalla K.H., Proepper C., Bockmann J., Sobue K., Gundelfinger E.D., Kreutz M.R., Boeckers T.M.
    J. Biol. Chem. 281:13805-13816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LZTS3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Abelson interacting protein 1 (Abi-1) is essential for dendrite morphogenesis and synapse formation."
    Proepper C., Johannsen S., Liebau S., Dahl J., Vaida B., Bockmann J., Kreutz M.R., Gundelfinger E.D., Boeckers T.M.
    EMBO J. 26:1397-1409(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ABI1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-677; PRO-678; PRO-679; PRO-680 AND PRO-684.
  9. "Importance of Shank3 protein in regulating metabotropic glutamate receptor 5 (mGluR5) expression and signaling at synapses."
    Verpelli C., Dvoretskova E., Vicidomini C., Rossi F., Chiappalone M., Schoen M., Di Stefano B., Mantegazza R., Broccoli V., Boeckers T.M., Dityatev A., Sala C.
    J. Biol. Chem. 286:34839-34850(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MGLUR5 SIGNALING REGULATION, TISSUE SPECIFICITY.
  10. "Autism-associated mutations in ProSAP2/Shank3 impair synaptic transmission and neurexin-neuroligin-mediated transsynaptic signaling."
    Arons M.H., Thynne C.J., Grabrucker A.M., Li D., Schoen M., Cheyne J.E., Boeckers T.M., Montgomery J.M., Garner C.C.
    J. Neurosci. 32:14966-14978(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-12; ARG-300 AND GLN-321.
  11. "SHANK3 mutations identified in autism lead to modification of dendritic spine morphology via an actin-dependent mechanism."
    Durand C.M., Perroy J., Loll F., Perrais D., Fagni L., Bourgeron T., Montcouquiol M., Sans N.
    Mol. Psychiatry 17:71-84(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACTIN-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-12; ARG-300 AND GLN-321.
  12. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-387; SER-394; TYR-931; THR-1131; SER-1135; SER-1160; SER-1167; THR-1235; SER-1254; SER-1421; SER-1511 AND SER-1644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "SHANK3 gene mutations associated with autism facilitate ligand binding to the Shank3 ankyrin repeat region."
    Mameza M.G., Dvoretskova E., Bamann M., Hoenck H.H., Gueler T., Boeckers T.M., Schoen M., Verpelli C., Sala C., Barsukov I., Dityatev A., Kreienkamp H.J.
    J. Biol. Chem. 288:26697-26708(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH SHARPIN AND SPTAN1, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-68; ARG-300 AND GLN-321.
  14. "Shank3 deficiency induces NMDA receptor hypofunction via an actin-dependent mechanism."
    Duffney L.J., Wei J., Cheng J., Liu W., Smith K.R., Kittler J.T., Yan Z.
    J. Neurosci. 33:15767-15778(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NMDA RECEPTOR SIGNALING REGULATION.
  15. "An architectural framework that may lie at the core of the postsynaptic density."
    Baron M.K., Boeckers T.M., Vaida B., Faham S., Gingery M., Sawaya M.R., Salyer D., Gundelfinger E.D., Bowie J.U.
    Science 311:531-535(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1674-1740.

Entry informationi

Entry nameiSHAN3_RAT
AccessioniPrimary (citable) accession number: Q9JLU4
Secondary accession number(s): Q9WUY7, Q9WV47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: February 19, 2014
Last modified: May 11, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.