Q9JLU4 (SHAN3_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Shank3

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1815 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that 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. May play a role in the structural and functional organization of the dendritic spine and synaptic junction.
Subunit structure	May homomultimerize via its SAM domain. Interacts with BAIAP2 By similarity. Interacts with DLGAP1/GKAP, MGLUR1A and MGLUR5 C-termini via its PDZ domain. Interacts with HOMER1, HOMER2, HOMER3 and CTTN/cortactin SH3 domain. Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts with DBNL. Interacts (via PDZ domain) with PROSAPIP1 (via C-terminus). Ref.1 Ref.2 Ref.4 Ref.6 Ref.7
Subcellular location	Cytoplasm. Cell junction › synapse. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density. Note: Postsynaptic density of neuronal cells. Extends into the region subjacent to the PSD. Ref.7
Tissue specificity	Detected in brain (at protein level). Widely expressed in brain. Ref.6 Ref.7
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.
Caution	It is uncertain whether Met-1 or Met-76 is the initiator.
Sequence caution	The sequence AAD42976.1 differs from that shown. Reason: Frameshift at positions 973 and 1000. The sequence AAF61375.1 differs from that shown. Reason: Frameshift at positions 3 and 37.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Coiled coil Repeat SH3 domain SH3-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from electronic annotation. Source: Compara N-methyl-D-aspartate receptor clustering Inferred from electronic annotation. Source: Compara alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor clustering Inferred from sequence or structural similarity PubMed 21795692. Source: BHF-UCL brain morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL dendritic spine morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL embryonic epithelial tube formation Inferred from electronic annotation. Source: Compara guanylate kinase-associated protein clustering Inferred from electronic annotation. Source: Compara learning Inferred from electronic annotation. Source: Compara locomotory exploration behavior Inferred from sequence or structural similarity. Source: BHF-UCL memory Inferred from electronic annotation. Source: Compara negative regulation of actin filament bundle assembly Inferred from electronic annotation. Source: Compara negative regulation of cell volume Inferred from sequence or structural similarity. Source: BHF-UCL neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of dendritic spine development Inferred from sequence or structural similarity PubMed 21795692. Source: BHF-UCL positive regulation of excitatory postsynaptic membrane potential Inferred from sequence or structural similarity PubMed 21795692. Source: BHF-UCL positive regulation of glutamate receptor signaling pathway Inferred from sequence or structural similarity PubMed 21795692. Source: BHF-UCL positive regulation of long-term neuronal synaptic plasticity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synapse structural plasticity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of synaptic transmission, glutamatergic Inferred from sequence or structural similarity PubMed 21795692. Source: BHF-UCL postsynaptic density assembly Inferred from sequence or structural similarity. Source: BHF-UCL protein oligomerization Inferred from direct assay Ref.8. Source: RGD regulation of behavioral fear response Inferred from sequence or structural similarity. Source: BHF-UCL regulation of dendritic spine morphogenesis Inferred from sequence or structural similarity PubMed 21795692. Source: BHF-UCL regulation of grooming behavior Inferred from electronic annotation. Source: Compara regulation of long term synaptic depression Inferred from sequence or structural similarity PubMed 21795692. Source: BHF-UCL regulation of long-term synaptic potentiation Inferred from electronic annotation. Source: Compara social behavior Inferred from sequence or structural similarity. Source: BHF-UCL striatal medium spiny neuron differentiation Inferred from sequence or structural similarity. Source: BHF-UCL vocalization behavior Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cilium membrane Inferred from direct assay PubMed 18596612. Source: BHF-UCL cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from direct assay Ref.7. Source: UniProtKB postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	GKAP/Homer scaffold activity Inferred from direct assay Ref.4. Source: BHF-UCL ionotropic glutamate receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL protein self-association Inferred from direct assay Ref.8. Source: RGD zinc ion binding Inferred from direct assay Ref.8. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-6271152,EBI-6271152

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: Q9JLU4-1)

Also known as: A;

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 1 (identifier: Q9JLU4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1612-1620: Missing.

Isoform 3 (identifier: Q9JLU4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1204-1211: SPTPVHSP → PRRRAGMV
     1212-1815: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1815

1815

SH3 and multiple ankyrin repeat domains protein 3

PRO_0000174676

Regions

Repeat

223 – 256

34

ANK 1

Repeat

257 – 289

33

ANK 2

Repeat

290 – 320

31

ANK 3

Repeat

324 – 353

30

ANK 4

Repeat

357 – 386

30

ANK 5

Repeat

390 – 420

31

ANK 6

Domain

545 – 604

60

SH3

Domain

645 – 739

95

PDZ

Domain

1752 – 1815

64

SAM

Coiled coil

1570 – 1590

21

Potential

Motif

1486 – 1492

7

SH3-binding Potential

Compositional bias

6 – 15

10

Poly-Ala

Compositional bias

895 – 901

7

Poly-Pro

Compositional bias

914 – 919

6

Poly-Pro

Amino acid modifications

Modified residue

197

1

Phosphotyrosine By similarity

Modified residue

450

1

Phosphoserine By similarity

Modified residue

469

1

Phosphoserine By similarity

Modified residue

630

1

Phosphotyrosine By similarity

Modified residue

639

1

Phosphotyrosine By similarity

Modified residue

856

1

Phosphoserine By similarity

Modified residue

1235

1

Phosphoserine By similarity

Modified residue

1239

1

Phosphoserine By similarity

Modified residue

1310

1

Phosphothreonine By similarity

Modified residue

1329

1

Phosphoserine By similarity

Modified residue

1719

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1204 – 1211

8

SPTPVHSP → PRRRAGMV in isoform 3.

VSP_006087

Alternative sequence

1212 – 1815

604

Missing in isoform 3.

VSP_006088

Alternative sequence

1612 – 1620

9

Missing in isoform 1.

VSP_006089

Experimental info

Mutagenesis

1386

1

P → L: Abolishes interaction with HOMER1 isoform 3. Ref.4

Mutagenesis

1389

1

F → C: Abolishes interaction with HOMER1 isoform 3. Ref.4

Sequence conflict

1 – 2

2

MQ → AA Ref.2

Sequence conflict

32

1

P → Y Ref.2

Sequence conflict

37

1

R → Q Ref.2

Sequence conflict

68

1

Q → P Ref.2

Sequence conflict

472

1

H → L in AAD42976. Ref.3

Sequence conflict

781

1

R → G in AAD42976. Ref.3

Sequence conflict

902 – 907

6

YYFDSG → ILRLR in AAD42976. Ref.3

Sequence conflict

912 – 917

6

FSPPPP → SHHGHQ in AAD42976. Ref.3

Sequence conflict

921

1

R → G in AAD42976. Ref.3

Sequence conflict

963

1

R → G in AAD42976. Ref.3

Sequence conflict

1115

1

S → N in AAF61375. Ref.2

Sequence conflict

1162

1

S → N in AAF61375. Ref.2

Sequence conflict

1167

1

G → S in AAF61375. Ref.2

Sequence conflict

1337

1

S → N in AAF61375. Ref.2

Sequence conflict

1345

1

G → S in AAF61375. Ref.2

Sequence conflict

1348

1

S → N in AAF61375. Ref.2

Sequence conflict

1354

1

E → K in AAF61375. Ref.2

Sequence conflict

1369

1

S → N in AAF61375. Ref.2

Sequence conflict

1507

1

D → G in AAF61375. Ref.2

Sequence conflict

1715

1

V → A in AAF61375. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1815

Helix Strand Turn

Details...

Helix

1749 – 1751

3

Helix

1754 – 1763

10

Helix

1767 – 1769

3

Helix

1770 – 1775

6

Helix

1780 – 1785

6

Helix

1788 – 1793

6

Helix

1799 – 1810

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (A) [UniParc]. Last modified July 26, 2002. Version 2. Checksum: 6632CF8F040766F9	FASTA	1,815	193,258
	10 20 30 40 50 60 MQLNRAAVAA AAAPAEPPEP LSPALAPAPA PPGPLPRSAV GGTLAGGQGG PGRRAESPCA 70 80 90 100 110 120 PLSAGNSQGP GASTGMDGPG ASAVVVRVGI PDLQQTKCLR LDPTAPVWAA KQRVLCALNH 130 140 150 160 170 180 SLQDALNYGL FQPPSRGRAG KFLDEERLLQ DYPPNLDTPL PYLEFRYKRR VYAQNLIDDK 190 200 210 220 230 240 QFAKLHTKAN LKKFMDYVQL HSTDKVARLL DKGLDPNFHD PDSGECPLSL AAQLDNATDL 250 260 270 280 290 300 LKVLRNGGAH LDFRTRDGLT AVHCATRQRN AGALTTLLDL GASPDYKDSR GLTPLYHSAL 310 320 330 340 350 360 GGGDALCCEL LLHDHAQLGT TDENGWQEIH QACRFGHVQH LEHLLFYGAN MGAQNASGNT 370 380 390 400 410 420 ALHICALYNQ ESCARVLLFR GANKDVRNYN SQTAFQVAII AGNFELAEVI KTHKDSDVVP 430 440 450 460 470 480 FRETPSYAKR RRLAGPSGLA SPRPLQRSAS DINLKGDQPA ASPGPTLRSL PHQLLLQRLQ 490 500 510 520 530 540 EEKDRDRDGE QENDISGPSA GRGGHSKISP SGPGGSGPAP GPGPASPAPP APPPRGPKRK 550 560 570 580 590 600 LYSAVPGRKF IAVKAHSPQG EGEIPLHRGE AVKVLSIGEG GFWEGTVKGR TGWFPADCVE 610 620 630 640 650 660 EVQMRQYDTR HETREDRTKR LFRHYTVGSY DSLTSHSDYV IDDKVAILQK RDHEGFGFVL 670 680 690 700 710 720 RGAKAETPIE EFTPTPAFPA LQYLESVDVE GVAWKAGLRT GDFLIEVNGV NVVKVGHKQV 730 740 750 760 770 780 VGLIRQGGNR LVMKVVSVTR KPEEDSARRR APPPPKRAPS TTLTLRSKSM TAELEELASI 790 800 810 820 830 840 RRRKGEKLDE ILAVAAEPTL RPDIADADSR AATVKQRPTS RRITPAEISS LFERQGLPGP 850 860 870 880 890 900 EKLPGSLRKG IPRTKSVGED EKLASLLEGR FPRSTSMQDT VREGRGIPPP PQTAPPPPPA 910 920 930 940 950 960 PYYFDSGPPP TFSPPPPPPG RAYDTVRSSF KPGLEARLGA GAAGLYDSGT PLGPLPYPER 970 980 990 1000 1010 1020 QKRARSMIIL QDSAPEVGDV PRPAPAATPP ERPKRRPRPS GPDSPYANLG AFSASLFAPS 1030 1040 1050 1060 1070 1080 KPQRRKSPLV KQLQVEDAQE RAALAVGSPG PVGGSFAREP SPTHRGPRPG GLDYSSGEGL 1090 1100 1110 1120 1130 1140 GLTFGGPSPG PVKERRLEER RRSTVFLSVG AIEGSPPSAD LPSLQPSRSI DERLLGTGAT 1150 1160 1170 1180 1190 1200 TGRDLLLPSP VSALKPLVGG PSLGPSGSTF IHPLTGKPLD PSSPLALALA ARERALASQT 1210 1220 1230 1240 1250 1260 PSRSPTPVHS PDADRPGPLF VDVQTRDSER GPLASPAFSP RSPAWIPVPA RREAEKPTRE 1270 1280 1290 1300 1310 1320 ERKSPEDKKS MILSVLDTSL QRPAGLIVVH ATSNGQEPNR LGAEEERPGT PELAPTPMQA 1330 1340 1350 1360 1370 1380 AAVAEPMPSP RAQPPGSIPA DPGPGQGSSE EEPELVFAVN LPPAQLSSSD EETREELARI 1390 1400 1410 1420 1430 1440 GLVPPPEEFA NGILLATPPP GPGPLPTTVP SPASGKPSSE LPPAPESAAD SGVEEADTRS 1450 1460 1470 1480 1490 1500 SSDPHLETTS TISTVSSMST LSSESGELTD THTSFADGHT FLLEKPPVPP KPKLKSPLGK 1510 1520 1530 1540 1550 1560 GPVTFRDPLL KQSSDSELMA QQHHATSTGL TSAAGPARPR YLFQRRSKLW GDPVESRGLP 1570 1580 1590 1600 1610 1620 GPEDDKPTVI SELSSRLQQL NKDTRSLGEE PVGGLGSLLD PAKKSPIAAA RCAVVPSAGW 1630 1640 1650 1660 1670 1680 LFSSLGELST ISAQRSPGGP GGGASYSVRP SGRYPVARRA PSPVKPASLE RVEGLGAGVG 1690 1700 1710 1720 1730 1740 GAGRPFGLTP PTILKSSSLS IPHEPKEVRF VVRSVSARSR SPSPSPLPSP SPGSGPSAGP 1750 1760 1770 1780 1790 1800 RRPFQQKPLQ LWSKFDVGDW LESIHLGEHR DRFEDHEIEG AHLPALTKED FVELGVTRVG 1810 HRMNIERALR QLDGS
	Isoform 1 [UniParc]. Checksum: 4CC8A0E049C1B094	FASTA	1,806	192,387
	10 20 30 40 50 60 MQLNRAAVAA AAAPAEPPEP LSPALAPAPA PPGPLPRSAV GGTLAGGQGG PGRRAESPCA 70 80 90 100 110 120 PLSAGNSQGP GASTGMDGPG ASAVVVRVGI PDLQQTKCLR LDPTAPVWAA KQRVLCALNH 130 140 150 160 170 180 SLQDALNYGL FQPPSRGRAG KFLDEERLLQ DYPPNLDTPL PYLEFRYKRR VYAQNLIDDK 190 200 210 220 230 240 QFAKLHTKAN LKKFMDYVQL HSTDKVARLL DKGLDPNFHD PDSGECPLSL AAQLDNATDL 250 260 270 280 290 300 LKVLRNGGAH LDFRTRDGLT AVHCATRQRN AGALTTLLDL GASPDYKDSR GLTPLYHSAL 310 320 330 340 350 360 GGGDALCCEL LLHDHAQLGT TDENGWQEIH QACRFGHVQH LEHLLFYGAN MGAQNASGNT 370 380 390 400 410 420 ALHICALYNQ ESCARVLLFR GANKDVRNYN SQTAFQVAII AGNFELAEVI KTHKDSDVVP 430 440 450 460 470 480 FRETPSYAKR RRLAGPSGLA SPRPLQRSAS DINLKGDQPA ASPGPTLRSL PHQLLLQRLQ 490 500 510 520 530 540 EEKDRDRDGE QENDISGPSA GRGGHSKISP SGPGGSGPAP GPGPASPAPP APPPRGPKRK 550 560 570 580 590 600 LYSAVPGRKF IAVKAHSPQG EGEIPLHRGE AVKVLSIGEG GFWEGTVKGR TGWFPADCVE 610 620 630 640 650 660 EVQMRQYDTR HETREDRTKR LFRHYTVGSY DSLTSHSDYV IDDKVAILQK RDHEGFGFVL 670 680 690 700 710 720 RGAKAETPIE EFTPTPAFPA LQYLESVDVE GVAWKAGLRT GDFLIEVNGV NVVKVGHKQV 730 740 750 760 770 780 VGLIRQGGNR LVMKVVSVTR KPEEDSARRR APPPPKRAPS TTLTLRSKSM TAELEELASI 790 800 810 820 830 840 RRRKGEKLDE ILAVAAEPTL RPDIADADSR AATVKQRPTS RRITPAEISS LFERQGLPGP 850 860 870 880 890 900 EKLPGSLRKG IPRTKSVGED EKLASLLEGR FPRSTSMQDT VREGRGIPPP PQTAPPPPPA 910 920 930 940 950 960 PYYFDSGPPP TFSPPPPPPG RAYDTVRSSF KPGLEARLGA GAAGLYDSGT PLGPLPYPER 970 980 990 1000 1010 1020 QKRARSMIIL QDSAPEVGDV PRPAPAATPP ERPKRRPRPS GPDSPYANLG AFSASLFAPS 1030 1040 1050 1060 1070 1080 KPQRRKSPLV KQLQVEDAQE RAALAVGSPG PVGGSFAREP SPTHRGPRPG GLDYSSGEGL 1090 1100 1110 1120 1130 1140 GLTFGGPSPG PVKERRLEER RRSTVFLSVG AIEGSPPSAD LPSLQPSRSI DERLLGTGAT 1150 1160 1170 1180 1190 1200 TGRDLLLPSP VSALKPLVGG PSLGPSGSTF IHPLTGKPLD PSSPLALALA ARERALASQT 1210 1220 1230 1240 1250 1260 PSRSPTPVHS PDADRPGPLF VDVQTRDSER GPLASPAFSP RSPAWIPVPA RREAEKPTRE 1270 1280 1290 1300 1310 1320 ERKSPEDKKS MILSVLDTSL QRPAGLIVVH ATSNGQEPNR LGAEEERPGT PELAPTPMQA 1330 1340 1350 1360 1370 1380 AAVAEPMPSP RAQPPGSIPA DPGPGQGSSE EEPELVFAVN LPPAQLSSSD EETREELARI 1390 1400 1410 1420 1430 1440 GLVPPPEEFA NGILLATPPP GPGPLPTTVP SPASGKPSSE LPPAPESAAD SGVEEADTRS 1450 1460 1470 1480 1490 1500 SSDPHLETTS TISTVSSMST LSSESGELTD THTSFADGHT FLLEKPPVPP KPKLKSPLGK 1510 1520 1530 1540 1550 1560 GPVTFRDPLL KQSSDSELMA QQHHATSTGL TSAAGPARPR YLFQRRSKLW GDPVESRGLP 1570 1580 1590 1600 1610 1620 GPEDDKPTVI SELSSRLQQL NKDTRSLGEE PVGGLGSLLD PAKKSPIAAA RLFSSLGELS 1630 1640 1650 1660 1670 1680 TISAQRSPGG PGGGASYSVR PSGRYPVARR APSPVKPASL ERVEGLGAGV GGAGRPFGLT 1690 1700 1710 1720 1730 1740 PPTILKSSSL SIPHEPKEVR FVVRSVSARS RSPSPSPLPS PSPGSGPSAG PRRPFQQKPL 1750 1760 1770 1780 1790 1800 QLWSKFDVGD WLESIHLGEH RDRFEDHEIE GAHLPALTKE DFVELGVTRV GHRMNIERAL RQLDGS
	Isoform 3 [UniParc]. Checksum: A9B2F833ED29460A	FASTA	1,211	129,576
	10 20 30 40 50 60 MQLNRAAVAA AAAPAEPPEP LSPALAPAPA PPGPLPRSAV GGTLAGGQGG PGRRAESPCA 70 80 90 100 110 120 PLSAGNSQGP GASTGMDGPG ASAVVVRVGI PDLQQTKCLR LDPTAPVWAA KQRVLCALNH 130 140 150 160 170 180 SLQDALNYGL FQPPSRGRAG KFLDEERLLQ DYPPNLDTPL PYLEFRYKRR VYAQNLIDDK 190 200 210 220 230 240 QFAKLHTKAN LKKFMDYVQL HSTDKVARLL DKGLDPNFHD PDSGECPLSL AAQLDNATDL 250 260 270 280 290 300 LKVLRNGGAH LDFRTRDGLT AVHCATRQRN AGALTTLLDL GASPDYKDSR GLTPLYHSAL 310 320 330 340 350 360 GGGDALCCEL LLHDHAQLGT TDENGWQEIH QACRFGHVQH LEHLLFYGAN MGAQNASGNT 370 380 390 400 410 420 ALHICALYNQ ESCARVLLFR GANKDVRNYN SQTAFQVAII AGNFELAEVI KTHKDSDVVP 430 440 450 460 470 480 FRETPSYAKR RRLAGPSGLA SPRPLQRSAS DINLKGDQPA ASPGPTLRSL PHQLLLQRLQ 490 500 510 520 530 540 EEKDRDRDGE QENDISGPSA GRGGHSKISP SGPGGSGPAP GPGPASPAPP APPPRGPKRK 550 560 570 580 590 600 LYSAVPGRKF IAVKAHSPQG EGEIPLHRGE AVKVLSIGEG GFWEGTVKGR TGWFPADCVE 610 620 630 640 650 660 EVQMRQYDTR HETREDRTKR LFRHYTVGSY DSLTSHSDYV IDDKVAILQK RDHEGFGFVL 670 680 690 700 710 720 RGAKAETPIE EFTPTPAFPA LQYLESVDVE GVAWKAGLRT GDFLIEVNGV NVVKVGHKQV 730 740 750 760 770 780 VGLIRQGGNR LVMKVVSVTR KPEEDSARRR APPPPKRAPS TTLTLRSKSM TAELEELASI 790 800 810 820 830 840 RRRKGEKLDE ILAVAAEPTL RPDIADADSR AATVKQRPTS RRITPAEISS LFERQGLPGP 850 860 870 880 890 900 EKLPGSLRKG IPRTKSVGED EKLASLLEGR FPRSTSMQDT VREGRGIPPP PQTAPPPPPA 910 920 930 940 950 960 PYYFDSGPPP TFSPPPPPPG RAYDTVRSSF KPGLEARLGA GAAGLYDSGT PLGPLPYPER 970 980 990 1000 1010 1020 QKRARSMIIL QDSAPEVGDV PRPAPAATPP ERPKRRPRPS GPDSPYANLG AFSASLFAPS 1030 1040 1050 1060 1070 1080 KPQRRKSPLV KQLQVEDAQE RAALAVGSPG PVGGSFAREP SPTHRGPRPG GLDYSSGEGL 1090 1100 1110 1120 1130 1140 GLTFGGPSPG PVKERRLEER RRSTVFLSVG AIEGSPPSAD LPSLQPSRSI DERLLGTGAT 1150 1160 1170 1180 1190 1200 TGRDLLLPSP VSALKPLVGG PSLGPSGSTF IHPLTGKPLD PSSPLALALA ARERALASQT 1210 PSRPRRRAGM V

References

[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.
[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 2), INTERACTION WITH DLGAP1 AND CTTN. 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 (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-1386 AND PHE-1389.
[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 PROSAPIP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"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 1749-1815.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ133120 mRNA. Translation: CAB45688.1.
AF133301 mRNA. Translation: AAF61375.1. Frameshift.
AF159047 mRNA. Translation: AAD42976.1. Frameshift.

IPI

IPI00204088.
IPI00231141.
IPI00231142.

RefSeq

NP_067708.1. NM_021676.1.

UniGene

Rn.42876.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F3N	X-ray	2.10	A/B/C	1749-1815	[»]
2F44	X-ray	2.40	A/B/C	1749-1815	[»]

ProteinModelPortal

Q9JLU4.

SMR

Q9JLU4. Positions 638-740, 1749-1812.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1486849.

PTM databases

PhosphoSite

Q9JLU4.

Proteomic databases

PaxDb

Q9JLU4.

PRIDE

Q9JLU4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000045913; ENSRNOP00000040444; ENSRNOG00000032936.
ENSRNOT00000047960; ENSRNOP00000041083; ENSRNOG00000032936.

GeneID

59312.

KEGG

rno:59312.

Organism-specific databases

CTD

85358.

RGD

69264. Shank3.

Phylogenomic databases

eggNOG

COG0666.

GeneTree

ENSGT00510000046474.

HOGENOM

HOG000293276.

HOVERGEN

HBG054027.

InParanoid

Q9JLU4.

KO

K15009.

OrthoDB

EOG48PMJ9.

Gene expression databases

ArrayExpress

Q9JLU4.

Genevestigator

Q9JLU4.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
1.25.40.20. 1 hit.

InterPro

IPR002110. 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]

Pfam

PF12796. Ank_2. 2 hits.
PF00595. PDZ. 1 hit.
PF00536. SAM_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]

SMART

SM00248. ANK. 5 hits.
SM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.
SSF50156. PDZ. 1 hit.
SSF47769. SAM_homology. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS50297. 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]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9JLU4.

NextBio

611861.

Entry information

Entry name

SHAN3_RAT

Accession

Primary (citable) accession number: Q9JLU4
Secondary accession number(s): Q9WUY7, Q9WV47

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	July 26, 2002
Last modified:	April 3, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program