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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
  • 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

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

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
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi12R → C: Disrupts postsynaptic AMPA and NMDA receptor-mediated synaptic transmission as well as transsynaptic signaling and spine maturation. 2 Publications1
Mutagenesisi68L → P: Slightly increases interaction with SHARPIN and SPTAN1. No effect on localization. 1 Publication1
Mutagenesisi300R → 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 Publications1
Mutagenesisi321Q → 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 Publications1
Mutagenesisi677P → A: Strongly decreases interaction with ABI1. 1 Publication1
Mutagenesisi678P → A: Almost abolishes interaction with ABI1. 1 Publication1
Mutagenesisi679P → A: Abolishes interaction with ABI1. 1 Publication1
Mutagenesisi680P → A: Abolishes interaction with ABI1. 1 Publication1
Mutagenesisi684P → A: Abolishes interaction with ABI1. 1 Publication1
Mutagenesisi1311P → L: Abolishes interaction with HOMER1 isoform 3. 1 Publication1
Mutagenesisi1314F → C: Abolishes interaction with HOMER1 isoform 3. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001746761 – 1740SH3 and multiple ankyrin repeat domains protein 3Add BLAST1740

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei122PhosphotyrosineBy similarity1
Modified residuei373PhosphoserineBy similarity1
Modified residuei375PhosphoserineCombined sources1
Modified residuei387PhosphoserineCombined sources1
Modified residuei394PhosphoserineCombined sources1
Modified residuei482PhosphoserineBy similarity1
Modified residuei555PhosphotyrosineBy similarity1
Modified residuei694PhosphoserineBy similarity1
Modified residuei781PhosphoserineBy similarity1
Modified residuei790PhosphoserineBy similarity1
Modified residuei801PhosphoserineBy similarity1
Modified residuei891PhosphoserineBy similarity1
Modified residuei898PhosphoserineBy similarity1
Modified residuei913PhosphothreonineBy similarity1
Modified residuei931PhosphotyrosineCombined sources1
Modified residuei966Asymmetric dimethylarginineBy similarity1
Modified residuei1131PhosphothreonineCombined sources1
Modified residuei1135PhosphoserineCombined sources1
Modified residuei1160PhosphoserineCombined sources1
Modified residuei1164PhosphoserineBy similarity1
Modified residuei1167PhosphoserineCombined sources1
Modified residuei1235PhosphothreonineCombined sources1
Modified residuei1254PhosphoserineCombined sources1
Modified residuei1421PhosphoserineCombined sources1
Modified residuei1511PhosphoserineCombined sources1
Modified residuei1522PhosphoserineBy similarity1
Modified residuei1530PhosphoserineBy similarity1
Modified residuei1549PhosphoserineBy similarity1
Modified residuei1644PhosphoserineCombined sources1
Modified residuei1646PhosphoserineBy similarity1
Modified residuei1648PhosphoserineBy similarity1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ9JLU4.
PRIDEiQ9JLU4.

PTM databases

iPTMnetiQ9JLU4.
PhosphoSitePlusiQ9JLU4.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSRNOG00000032936.

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
  • 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 interactors.
IntActiQ9JLU4. 8 interactors.
MINTiMINT-1486849.
STRINGi10116.ENSRNOP00000041083.

Structurei

Secondary structure

11740
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1674 – 1676Combined sources3
Helixi1679 – 1688Combined sources10
Helixi1692 – 1694Combined sources3
Helixi1695 – 1700Combined sources6
Helixi1705 – 1710Combined sources6
Helixi1713 – 1718Combined sources6
Helixi1724 – 1735Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F3NX-ray2.10A/B/C1674-1740[»]
2F44X-ray2.40A/B/C1674-1740[»]
SMRiQ9JLU4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLU4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati148 – 181ANK 1Add BLAST34
Repeati182 – 214ANK 2Add BLAST33
Repeati215 – 245ANK 3Add BLAST31
Repeati249 – 278ANK 4Add BLAST30
Repeati282 – 311ANK 5Add BLAST30
Repeati315 – 345ANK 6Add BLAST31
Domaini470 – 529SH3PROSITE-ProRule annotationAdd BLAST60
Domaini570 – 664PDZPROSITE-ProRule annotationAdd BLAST95
Domaini1677 – 1740SAMPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 75Intramolecular interaction with the ANK repeatsAdd BLAST75
Regioni677 – 684Required for interaction with ABI11 Publication8

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1495 – 1515Sequence analysisAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1411 – 1417SH3-bindingSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi820 – 826Poly-Pro7
Compositional biasi839 – 844Poly-Pro6

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.

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 differs from that shown. Reason: Frameshift at positions 898 and 925.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti397H → L in AAD42976 (PubMed:10958799).Curated1
Sequence conflicti706R → G in AAD42976 (PubMed:10958799).Curated1
Sequence conflicti827 – 832YYFDSG → ILRLR in AAD42976 (PubMed:10958799).Curated6
Sequence conflicti837 – 842FSPPPP → SHHGHQ in AAD42976 (PubMed:10958799).Curated6
Sequence conflicti846R → G in AAD42976 (PubMed:10958799).Curated1
Sequence conflicti888R → G in AAD42976 (PubMed:10958799).Curated1
Sequence conflicti1040S → N in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1087S → N in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1092G → S in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1262S → N in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1270G → S in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1273S → N in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1279E → K in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1294S → N in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1432D → G in AAF61375 (PubMed:10433268).Curated1
Sequence conflicti1640V → A in AAF61375 (PubMed:10433268).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0060871129 – 1136SPTPVHSP → PRRRAGMV in isoform 3. Curated8
Alternative sequenceiVSP_0060881137 – 1740Missing in isoform 3. CuratedAdd BLAST604
Alternative sequenceiVSP_0060891537 – 1545Missing in isoform 1. 2 Publications9

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2F3NX-ray2.10A/B/C1674-1740[»]
2F44X-ray2.40A/B/C1674-1740[»]
SMRiQ9JLU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9JLU4.
PhosphoSitePlusiQ9JLU4.

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.

Enzyme and pathway databases

ReactomeiR-RNO-6794361. Interactions of neurexins and neuroligins at synapses.

Miscellaneous databases

EvolutionaryTraceiQ9JLU4.
PROiQ9JLU4.

Gene expression databases

BgeeiENSRNOG00000032936.

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...

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: November 2, 2016
This is version 150 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.