Q9BYB0 (SHAN3_HUMAN) 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

Gene names

Name:	SHANK3
Synonyms:	KIAA1650, PSAP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1741 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 By similarity. Interacts with DLGAP1/GKAP, MGLUR1A, MGLUR5 C-termini via its PDZ domain By similarity. Interacts with HOMER1, HOMER2, HOMER3 and CTTN/cortactin SH3 domain By similarity. Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts with DBNL. Interacts (via PDZ domain) with PROSAPIP1 (via C-terminus) By similarity. Interacts with BAIAP2. Ref.6
Subcellular location	Cytoplasm By similarity. Cell junction › synapse By similarity. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Note: Postsynaptic density of neuronal cells By similarity.
Tissue specificity	Expressed in the cerebral cortex and the cerebellum.
Involvement in disease	A chromosomal aberration involving SHANK3 is found in patients with chromosome 22q13.3 deletion syndrome. Translocation t(12;22)(q24.1;q13.3) with APPL2/DIP13B. Defects in SHANK3 are associated with autism spectrum disorders (ASD). ASD are characterized by impairments in reciprocal social interaction and communication as well as restricted and stereotyped patterns of interest and activities. ASD include forms with moderate to severe cognitive impairment and milder forms with higher cognitive ability (Asperger syndrome). Ref.7 Schizophrenia 15 (SCZD15) [MIM:613950]: A complex, multifactorial psychotic disorder or group of disorders characterized by disturbances in the form and content of thought (e.g. delusions, hallucinations), in mood (e.g. inappropriate affect), in sense of self and relationship to the external world (e.g. loss of ego boundaries, withdrawal), and in behavior (e.g bizarre or apparently purposeless behavior). Although it affects emotions, it is distinguished from mood disorders in which such disturbances are primary. Similarly, there may be mild impairment of cognitive function, and it is distinguished from the dementias in which disturbed cognitive function is considered primary. Some patients manifest schizophrenic as well as bipolar disorder symptoms and are often given the diagnosis of schizoaffective disorder. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10
Sequence similarities	Contains 6 ANK repeats. Contains 1 PDZ (DHR) domain. Contains 1 SAM (sterile alpha motif) domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cytoplasm Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation Schizophrenia
Domain	ANK repeat Coiled coil Repeat SH3 domain SH3-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-methyl-D-aspartate receptor clustering Inferred from sequence or structural similarity. Source: BHF-UCL 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 guanylate kinase-associated protein clustering Inferred from sequence or structural similarity. Source: BHF-UCL learning Inferred from sequence or structural similarity. Source: BHF-UCL locomotory exploration behavior Inferred from sequence or structural similarity PubMed 21423165. Source: BHF-UCL memory Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of cell volume Inferred from sequence or structural similarity. Source: BHF-UCL neuromuscular process controlling balance Inferred from sequence or structural similarity. Source: BHF-UCL 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 regulation of behavioral fear response Inferred from sequence or structural similarity PubMed 21423165. Source: BHF-UCL regulation of dendritic spine morphogenesis Inferred from sequence or structural similarity PubMed 21795692. Source: BHF-UCL 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 sequence or structural similarity. Source: BHF-UCL 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 PubMed 21167025. Source: BHF-UCL
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cilium membrane Inferred from sequence or structural similarity. Source: BHF-UCL cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from sequence or structural similarity. Source: BHF-UCL postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	GKAP/Homer scaffold activity Inferred from sequence or structural similarity. Source: BHF-UCL ionotropic glutamate receptor binding Inferred from sequence or structural similarity. Source: BHF-UCL protein C-terminus binding Inferred from sequence or structural similarity. Source: BHF-UCL scaffold protein binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	2	EBI-1752330,EBI-401755
NCK1	P16333	4	EBI-1752330,EBI-389883
PLCG1	P19174	2	EBI-1752330,EBI-79387

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BYB0-1)

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: Q9BYB0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1536-1544: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1741	1741	SH3 and multiple ankyrin repeat domains protein 3		PRO_0000174675
Regions
	Repeat	148 – 178	31	ANK 1
	Repeat	182 – 211	30	ANK 2
	Repeat	215 – 245	31	ANK 3
	Repeat	249 – 278	30	ANK 4
	Repeat	282 – 311	30	ANK 5
	Repeat	315 – 345	31	ANK 6
	Domain	472 – 531	60	SH3
	Domain	572 – 666	95	PDZ
	Domain	1678 – 1741	64	SAM
	Coiled coil	1495 – 1515	21	Potential
	Motif	1411 – 1417	7	SH3-binding Potential
	Compositional bias	679 – 682	4	Poly-Pro
	Compositional bias	720 – 723	4	Poly-Ala
	Compositional bias	815 – 931	117	Pro-rich
	Compositional bias	1233 – 1350	118	Pro-rich
Amino acid modifications
	Modified residue	122	1	Phosphotyrosine By similarity
	Modified residue	375	1	Phosphoserine By similarity
	Modified residue	395	1	Phosphoserine By similarity
	Modified residue	557	1	Phosphotyrosine By similarity
	Modified residue	566	1	Phosphotyrosine By similarity
	Modified residue	783	1	Phosphoserine By similarity
	Modified residue	1159	1	Phosphoserine Ref.8
	Modified residue	1163	1	Phosphoserine Ref.8
	Modified residue	1235	1	Phosphothreonine Ref.9
	Modified residue	1254	1	Phosphoserine Ref.9
	Modified residue	1644	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1536 – 1544	9	Missing in isoform 2.		VSP_026160
	Natural variant	12	1	R → C. Ref.7		VAR_032804
	Natural variant	198	1	A → G. Ref.7		VAR_032805
	Natural variant	224	1	A → T. Ref.7		VAR_032806
	Natural variant	245	1	I → T. Ref.10 Corresponds to variant rs9616915 [ dbSNP | Ensembl ].		VAR_032807
	Natural variant	300	1	R → C. Ref.7		VAR_032808
	Natural variant	494	1	H → Q. Ref.10		VAR_065799
	Natural variant	537	1	R → W in SCZD15. Ref.10		VAR_065800
	Natural variant	721	1	A → T. Ref.10		VAR_065801
	Natural variant	953	1	S → T. Ref.10		VAR_065802
	Natural variant	1011	1	G → V. Ref.10		VAR_065803
	Natural variant	1135	1	P → H.		VAR_065804
	Natural variant	1299	1	R → K. Ref.10		VAR_065805
	Natural variant	1334	1	V → G. Ref.10		VAR_065806
	Natural variant	1556	1	I → V. Ref.10		VAR_065807
	Natural variant	1655	1	P → T. Ref.10		VAR_065808

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 12, 2007. Version 2. Checksum: 0CC40F1F53E6F6D4	FASTA	1,741	186,295
	10 20 30 40 50 60 MDGPGASAVV VRVGIPDLQQ TKCLRLDPAA PVWAAKQRVL CALNHSLQDA LNYGLFQPPS 70 80 90 100 110 120 RGRAGKFLDE ERLLQEYPPN LDTPLPYLEF RYKRRVYAQN LIDDKQFAKL HTKANLKKFM 130 140 150 160 170 180 DYVQLHSTDK VARLLDKGLD PNFHDPDSGE CPLSLAAQLD NATDLLKVLK NGGAHLDFRT 190 200 210 220 230 240 RDGLTAVHCA TRQRNAAALT TLLDLGASPD YKDSRGLTPL YHSALGGGDA LCCELLLHDH 250 260 270 280 290 300 AQLGITDENG WQEIHQACRF GHVQHLEHLL FYGADMGAQN ASGNTALHIC ALYNQESCAR 310 320 330 340 350 360 VLLFRGANRD VRNYNSQTAF QVAIIAGNFE LAEVIKTHKD SDVVPFRETP SYAKRRRLAG 370 380 390 400 410 420 PSGLASPRPL QRSASDINLK GEAQPAASPG PSLRSLPHQL LLQRLQEEKD RDRDADQESN 430 440 450 460 470 480 ISGPLAGRAG QSKISEPGAP RSCIRIRARF PAPPAPPAPP PRGPKRKLYS AVPGRKFIAV 490 500 510 520 530 540 KAHSPQGEGE IPLHRGEAVK VLSIGEGGFW EGTVKGRTGW FPADCVEEVQ MRQHDTRPET 550 560 570 580 590 600 REDRTKRLFR HYTVGSYDSL TSHSDYVIDD KVAVLQKRDH EGFGFVLRGA KAETPIEEFT 610 620 630 640 650 660 PTPAFPALQY LESVDVEGVA WRAGLRTGDF LIEVNGVNVV KVGHKQVVAL IRQGGNRLVM 670 680 690 700 710 720 KVVSVTRKPE EDGARRRAPP PPKRAPSTTL TLRSKSMTAE LEELASIRRR KGEKLDEMLA 730 740 750 760 770 780 AAAEPTLRPD IADADSRAAT VKQRPTSRRI TPAEISSLFE RQGLPGPEKL PGSLRKGIPR 790 800 810 820 830 840 TKSVGEDEKL ASLLEGRFPR STSMQDPVRE GRGIPPPPQT APPPPPAPYY FDSGPPPAFS 850 860 870 880 890 900 PPPPPGRAYD TVRSSFKPGL EARLGAGAAG LYEPGAALGP LPYPERQKRA RSMIILQDSA 910 920 930 940 950 960 PESGDAPRPP PAATPPERPK RRPRPPGPDS PYANLGAFSA SLFAPSKPQR RKSPLVKQLQ 970 980 990 1000 1010 1020 VEDAQERAAL AVGSPGPGGG SFAREPSPTH RGPRPGGLDY GAGDGPGLAF GGPGPAKDRR 1030 1040 1050 1060 1070 1080 LEERRRSTVF LSVGAIEGSA PGADLPSLQP SRSIDERLLG TGPTAGRDLL LPSPVSALKP 1090 1100 1110 1120 1130 1140 LVSGPSLGPS GSTFIHPLTG KPLDPSSPLA LALAARERAL ASQAPSRSPT PVHSPDADRP 1150 1160 1170 1180 1190 1200 GPLFVDVQAR DPERGSLASP AFSPRSPAWI PVPARREAEK VPREERKSPE DKKSMILSVL 1210 1220 1230 1240 1250 1260 DTSLQRPAGL IVVHATSNGQ EPSRLGGAEE ERPGTPELAP APMQSAAVAE PLPSPRAQPP 1270 1280 1290 1300 1310 1320 GGTPADAGPG QGSSEEEPEL VFAVNLPPAQ LSSSDEETRE ELARIGLVPP PEEFANGVLL 1330 1340 1350 1360 1370 1380 ATPLAGPGPS PTTVPSPASG KPSSEPPPAP ESAADSGVEE ADTRSSSDPH LETTSTISTV 1390 1400 1410 1420 1430 1440 SSMSTLSSES GELTDTHTSF ADGHTFLLEK PPVPPKPKLK SPLGKGPVTF RDPLLKQSSD 1450 1460 1470 1480 1490 1500 SELMAQQHHA ASAGLASAAG PARPRYLFQR RSKLWGDPVE SRGLPGPEDD KPTVISELSS 1510 1520 1530 1540 1550 1560 RLQQLNKDTR SLGEEPVGGL GSLLDPAKKS PIAAARCRSP MVGLRLFSSL GELSSISAQR 1570 1580 1590 1600 1610 1620 SPGGPGGGAS YSVRPSGRYP VARRAPSPVK PASLERVEGL GAGAGGAGRP FGLTPPTILK 1630 1640 1650 1660 1670 1680 SSSLSIPHEP KEVRFVVRSV SARSRSPSPS PLPSPASGPG PGAPGPRRPF QQKPLQLWSK 1690 1700 1710 1720 1730 1740 FDVGDWLESI HLGEHRDRFE DHEIEGAHLP ALTKDDFVEL GVTRVGHRMN IERALRQLDG S
	Isoform 2 [UniParc]. Checksum: E12CDA1DC84A9326	FASTA	1,732	185,295
	10 20 30 40 50 60 MDGPGASAVV VRVGIPDLQQ TKCLRLDPAA PVWAAKQRVL CALNHSLQDA LNYGLFQPPS 70 80 90 100 110 120 RGRAGKFLDE ERLLQEYPPN LDTPLPYLEF RYKRRVYAQN LIDDKQFAKL HTKANLKKFM 130 140 150 160 170 180 DYVQLHSTDK VARLLDKGLD PNFHDPDSGE CPLSLAAQLD NATDLLKVLK NGGAHLDFRT 190 200 210 220 230 240 RDGLTAVHCA TRQRNAAALT TLLDLGASPD YKDSRGLTPL YHSALGGGDA LCCELLLHDH 250 260 270 280 290 300 AQLGITDENG WQEIHQACRF GHVQHLEHLL FYGADMGAQN ASGNTALHIC ALYNQESCAR 310 320 330 340 350 360 VLLFRGANRD VRNYNSQTAF QVAIIAGNFE LAEVIKTHKD SDVVPFRETP SYAKRRRLAG 370 380 390 400 410 420 PSGLASPRPL QRSASDINLK GEAQPAASPG PSLRSLPHQL LLQRLQEEKD RDRDADQESN 430 440 450 460 470 480 ISGPLAGRAG QSKISEPGAP RSCIRIRARF PAPPAPPAPP PRGPKRKLYS AVPGRKFIAV 490 500 510 520 530 540 KAHSPQGEGE IPLHRGEAVK VLSIGEGGFW EGTVKGRTGW FPADCVEEVQ MRQHDTRPET 550 560 570 580 590 600 REDRTKRLFR HYTVGSYDSL TSHSDYVIDD KVAVLQKRDH EGFGFVLRGA KAETPIEEFT 610 620 630 640 650 660 PTPAFPALQY LESVDVEGVA WRAGLRTGDF LIEVNGVNVV KVGHKQVVAL IRQGGNRLVM 670 680 690 700 710 720 KVVSVTRKPE EDGARRRAPP PPKRAPSTTL TLRSKSMTAE LEELASIRRR KGEKLDEMLA 730 740 750 760 770 780 AAAEPTLRPD IADADSRAAT VKQRPTSRRI TPAEISSLFE RQGLPGPEKL PGSLRKGIPR 790 800 810 820 830 840 TKSVGEDEKL ASLLEGRFPR STSMQDPVRE GRGIPPPPQT APPPPPAPYY FDSGPPPAFS 850 860 870 880 890 900 PPPPPGRAYD TVRSSFKPGL EARLGAGAAG LYEPGAALGP LPYPERQKRA RSMIILQDSA 910 920 930 940 950 960 PESGDAPRPP PAATPPERPK RRPRPPGPDS PYANLGAFSA SLFAPSKPQR RKSPLVKQLQ 970 980 990 1000 1010 1020 VEDAQERAAL AVGSPGPGGG SFAREPSPTH RGPRPGGLDY GAGDGPGLAF GGPGPAKDRR 1030 1040 1050 1060 1070 1080 LEERRRSTVF LSVGAIEGSA PGADLPSLQP SRSIDERLLG TGPTAGRDLL LPSPVSALKP 1090 1100 1110 1120 1130 1140 LVSGPSLGPS GSTFIHPLTG KPLDPSSPLA LALAARERAL ASQAPSRSPT PVHSPDADRP 1150 1160 1170 1180 1190 1200 GPLFVDVQAR DPERGSLASP AFSPRSPAWI PVPARREAEK VPREERKSPE DKKSMILSVL 1210 1220 1230 1240 1250 1260 DTSLQRPAGL IVVHATSNGQ EPSRLGGAEE ERPGTPELAP APMQSAAVAE PLPSPRAQPP 1270 1280 1290 1300 1310 1320 GGTPADAGPG QGSSEEEPEL VFAVNLPPAQ LSSSDEETRE ELARIGLVPP PEEFANGVLL 1330 1340 1350 1360 1370 1380 ATPLAGPGPS PTTVPSPASG KPSSEPPPAP ESAADSGVEE ADTRSSSDPH LETTSTISTV 1390 1400 1410 1420 1430 1440 SSMSTLSSES GELTDTHTSF ADGHTFLLEK PPVPPKPKLK SPLGKGPVTF RDPLLKQSSD 1450 1460 1470 1480 1490 1500 SELMAQQHHA ASAGLASAAG PARPRYLFQR RSKLWGDPVE SRGLPGPEDD KPTVISELSS 1510 1520 1530 1540 1550 1560 RLQQLNKDTR SLGEEPVGGL GSLLDPAKKS PIAAARLFSS LGELSSISAQ RSPGGPGGGA 1570 1580 1590 1600 1610 1620 SYSVRPSGRY PVARRAPSPV KPASLERVEG LGAGAGGAGR PFGLTPPTIL KSSSLSIPHE 1630 1640 1650 1660 1670 1680 PKEVRFVVRS VSARSRSPSP SPLPSPASGP GPGAPGPRRP FQQKPLQLWS KFDVGDWLES 1690 1700 1710 1720 1730 IHLGEHRDRF EDHEIEGAHL PALTKDDFVE LGVTRVGHRM NIERALRQLD GS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping." Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O. DNA Res. 8:1-9(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 936-1741 (ISOFORM 2).
[3]	"The nucleotide sequence of a long cDNA clone isolated from human spleen." Ohara O., Nagase T., Kikuno R., Okumura K. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 963-1741 (ISOFORM 2). Tissue: Spleen.
[4]	"Disruption of the ProSAP2 gene in a t(12;22)(q24.1;q13.3) is associated with the 22q13.3 deletion syndrome." Bonaglia M.C., Giorda R., Borgatti R., Felisari G., Gagliardi C., Selicorni A., Zuffardi O. Am. J. Hum. Genet. 69:261-268(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH APPL2.
[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]	"The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42." Soltau M., Richter D., Kreienkamp H.-J. Mol. Cell. Neurosci. 21:575-583(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BAIAP2.
[7]	"Mutations in the gene encoding the synaptic scaffolding protein SHANK3 are associated with autism spectrum disorders." Durand C.M., Betancur C., Boeckers T.M., Bockmann J., Chaste P., Fauchereau F., Nygren G., Rastam M., Gillberg I.C., Anckarsaeter H., Sponheim E., Goubran-Botros H., Delorme R., Chabane N., Mouren-Simeoni M.-C., de Mas P., Bieth E., Roge B. , Heron D., Burglen L., Gillberg C., Leboyer M., Bourgeron T. Nat. Genet. 39:25-27(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN ASD, VARIANTS CYS-12; GLY-198; THR-224 AND CYS-300.
[8]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1159 AND SER-1163, MASS SPECTROMETRY. Tissue: Platelet.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1235 AND SER-1254, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"De novo mutations in the gene encoding the synaptic scaffolding protein SHANK3 in patients ascertained for schizophrenia." Gauthier J., Champagne N., Lafreniere R.G., Xiong L., Spiegelman D., Brustein E., Lapointe M., Peng H., Cote M., Noreau A., Hamdan F.F., Addington A.M., Rapoport J.L., Delisi L.E., Krebs M.O., Joober R., Fathalli F., Mouaffak F. , Haghighi A.P., Neri C., Dube M.P., Samuels M.E., Marineau C., Stone E.A., Awadalla P., Barker P.A., Carbonetto S., Drapeau P., Rouleau G.A. Proc. Natl. Acad. Sci. U.S.A. 107:7863-7868(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SCZD15 TRP-537, VARIANTS THR-245; GLN-494; THR-721; THR-953; VAL-1011; LYS-1299; GLY-1334; VAL-1556 AND THR-1655.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC000050 Genomic DNA. No translation available. AC000036 Genomic DNA. No translation available. AB051437 mRNA. Translation: BAB33320.1. AK074038 mRNA. Translation: BAB84864.1.
IPI	IPI00019794. IPI00847618.
RefSeq	NP_277052.1. NM_033517.1.
UniGene	Hs.149035.
3D structure databases
ProteinModelPortal	Q9BYB0.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-52267N.
IntAct	Q9BYB0. 27 interactions.
MINT	MINT-4134553.
STRING	9606.ENSP00000262795.
PTM databases
PhosphoSite	Q9BYB0.
Polymorphism databases
DMDM	148887434.
Proteomic databases
PaxDb	Q9BYB0.
PRIDE	Q9BYB0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	85358.
KEGG	hsa:85358.
UCSC	uc003bnf.1. human.
Organism-specific databases
CTD	85358.
GeneCards	GC22P051112.
HGNC	HGNC:14294. SHANK3.
MIM	606230. gene. 613950. phenotype.
neXtProt	NX_Q9BYB0.
Orphanet	106. Autism. 48652. Monosomy 22q13. 3140. Schizophrenia.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0666.
HOVERGEN	HBG054027.
InParanoid	Q9BYB0.
KO	K15009.
Enzyme and pathway databases
Pathway_Interaction_DB	ret_pathway. Signaling events regulated by Ret tyrosine kinase.
Gene expression databases
CleanEx	HS_SHANK3.
Genevestigator	Q9BYB0.
GermOnline	ENSG00000099882. Homo sapiens.
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
ChiTaRS	SHANK3. human.
GenomeRNAi	85358.
NextBio	75867.
SOURCE	Search...

Entry information

Entry name

SHAN3_HUMAN

Accession

Primary (citable) accession number: Q9BYB0
Secondary accession number(s): Q8TET3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	June 12, 2007
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.