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Q9WV48 (SHAN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SH3 and multiple ankyrin repeat domains protein 1

Short name=Shank1
Alternative name(s):
GKAP/SAPAP-interacting protein
SPANK-1
Somatostatin receptor-interacting protein
Short name=SSTR-interacting protein
Short name=SSTRIP
Synamon
Gene names
Name:Shank1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2167 AA.
Sequence statusComplete.
Protein existenceEvidence 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, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction. Overexpression promotes maturation of dendritic spines and the enlargement of spine heads via its ability to recruit Homer to postsynaptic sites, and enhances presynaptic function. Ref.9 Ref.12

Subunit structure

May homomultimerize via its SAM domain. Interacts with the C-terminus of SSTR2 via the PDZ domain. Interacts with SHARPIN, SPTAN1, HOMER1 and DLGAP1/GKAP. Part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts with BAIAP2 By similarity. Interacts with IGSF9. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.11 Ref.13

Subcellular location

Cytoplasm. Cell junctionsynapse. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Note: Colocalizes with alpha-latrotoxin receptor 1. Ref.6

Tissue specificity

Expressed only in brain (neuropil of cortex, CA1 region hippocampus and molecular layer of cerebellum).

Developmental stage

Expression increases from low levels at birth to high levels at 3-4 weeks before dropping slightly in adulthood. Expressed in the cortex and the molecular layer of the cerebellum at postnatal day 7. Isoform 2 expression does not change during development of both cortex and cerebellum. Isoform 4 expression decreases significantly during development of cortex but not cerebellum. Ref.4

Sequence similarities

Belongs to the SHANK family.

Contains 7 ANK repeats.

Contains 1 PDZ (DHR) domain.

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAD29417.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAF02498.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Repeat
SH3 domain
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult behavior

Inferred from electronic annotation. Source: Ensembl

associative learning

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

cytoskeletal anchoring at plasma membrane

Non-traceable author statement Ref.5. Source: UniProtKB

dendritic spine morphogenesis

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

determination of affect

Inferred from electronic annotation. Source: Ensembl

habituation

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

long-term memory

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

negative regulation of actin filament bundle assembly

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

neuromuscular process controlling balance

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

olfactory behavior

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

positive regulation of dendritic spine development

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of excitatory postsynaptic membrane potential

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

protein complex assembly

Inferred from direct assay Ref.6. Source: BHF-UCL

protein localization to synapse

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

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

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

righting reflex

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

social behavior

Inferred from electronic annotation. Source: Ensembl

synapse maturation

Inferred from direct assay Ref.12. Source: UniProtKB

vocalization behavior

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendrite

Non-traceable author statement Ref.5. Source: UniProtKB

dendritic spine

Inferred from direct assay PubMed 15496675. Source: BHF-UCL

excitatory synapse

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

intracellular

Non-traceable author statement Ref.5. Source: UniProtKB

ionotropic glutamate receptor complex

Inferred from electronic annotation. Source: Ensembl

neuron projection

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

neuronal postsynaptic density

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

plasma membrane

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

postsynaptic membrane

Inferred from direct assay Ref.3. Source: RGD

synapse

Inferred from direct assay PubMed 15496675. Source: BHF-UCL

   Molecular_functionGKAP/Homer scaffold activity

Inferred from direct assay Ref.6. Source: BHF-UCL

SH3 domain binding

Inferred from physical interaction PubMed 15496675. Source: BHF-UCL

ankyrin repeat binding

Inferred from physical interaction PubMed 15496675. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 15496675. Source: BHF-UCL

ionotropic glutamate receptor binding

Inferred from physical interaction PubMed 20171009. Source: RGD

protein C-terminus binding

Inferred from physical interaction Ref.3. Source: RGD

protein binding

Inferred from physical interaction Ref.2Ref.1Ref.8PubMed 12626503PubMed 19345194. Source: IntAct

protein complex binding

Inferred from physical interaction Ref.8. Source: RGD

receptor signaling complex scaffold activity

Inferred from direct assay Ref.3. Source: RGD

scaffold protein binding

Inferred from physical interaction Ref.6. Source: BHF-UCL

somatostatin receptor binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9WV48-1)

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: Q9WV48-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-614: Missing.
     615-654: SQEGRQESRS...PSLIDGIDSG → MALSAVGGGP...PRRRSVWYIY
Isoform 3 (identifier: Q9WV48-3)

The sequence of this isoform differs from the canonical sequence as follows:
     646-654: Missing.
Isoform 4 (identifier: Q9WV48-4)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     797-804: Missing.
Isoform 5 (identifier: Q9WV48-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1930-1943: LSEDSQTSLLSKPS → QYRIVVKSSDFGDF
     1944-2167: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21672167SH3 and multiple ankyrin repeat domains protein 1
PRO_0000174672

Regions

Repeat195 – 21016ANK 1
Repeat212 – 24534ANK 2
Repeat246 – 27833ANK 3
Repeat279 – 31234ANK 4
Repeat313 – 34533ANK 5
Repeat346 – 37833ANK 6
Repeat379 – 39517ANK 7
Domain554 – 61360SH3
Domain663 – 75795PDZ
Domain2104 – 216764SAM
Compositional bias929 – 9324Poly-Pro
Compositional bias1010 – 10156Poly-His
Compositional bias1022 – 10276Poly-His
Compositional bias1194 – 11996Poly-Gly
Compositional bias1850 – 186011Poly-Pro

Amino acid modifications

Modified residue1861Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 614614Missing in isoform 2.
VSP_006072
Alternative sequence615 – 65440SQEGR…GIDSG → MALSAVGGGPGGGALPQPPP ALSSSWPALGPRRRSVWYIY in isoform 2.
VSP_006073
Alternative sequence646 – 6549Missing in isoform 3.
VSP_006074
Alternative sequence797 – 8048Missing in isoform 4.
VSP_006075
Alternative sequence1930 – 194314LSEDS…LSKPS → QYRIVVKSSDFGDF in isoform 5.
VSP_006076
Alternative sequence1944 – 2167224Missing in isoform 5.
VSP_006077

Experimental info

Sequence conflict11411S → T in AAD04569. Ref.1
Sequence conflict11741S → N in AAD29417. Ref.2
Sequence conflict12461R → K in AAD04569. Ref.1
Sequence conflict13231A → T in AAD04569. Ref.1
Sequence conflict13311S → D in AAD04569. Ref.1
Sequence conflict17261S → N in AAD29417. Ref.2

Secondary structure

................... 2167
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1999. Version 1.
Checksum: 3F478B5A7B18BA86

FASTA2,167226,335
        10         20         30         40         50         60 
MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR 

        70         80         90        100        110        120 
SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF 

       130        140        150        160        170        180 
QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL 

       190        200        210        220        230        240 
KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI 

       250        260        270        280        290        300 
DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL 

       310        320        330        340        350        360 
LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE 

       370        380        390        400        410        420 
TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR 

       430        440        450        460        470        480 
RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGPQG QSQPSAPSTK 

       490        500        510        520        530        540 
LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS 

       550        560        570        580        590        600 
LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV 

       610        620        630        640        650        660 
GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSLIDG IDSGSDYIIK 

       670        680        690        700        710        720 
EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD 

       730        740        750        760        770        780 
FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA SQQAKRLPPP 

       790        800        810        820        830        840 
AISLRSKSMT SELEEMVSPW KKKIEYEQQP AAVPSMEKKR TVYQMALNKL DEILAAAQQT 

       850        860        870        880        890        900 
ISASESPGPG GLASLGKHRP KGFFATESSF DPHHRSQPSY DRPSFLPPGP GLMLRQKSIG 

       910        920        930        940        950        960 
AAEDDRPYLA PPAMKFSRSL SVPGSEDIPP PPTTSPPEPP YSTPPAPSSS GRLTPSPRGG 

       970        980        990       1000       1010       1020 
PFNPSSGGPL PASSPSSFDG PSPPDTRGGG REKSLYHSAA LPPAHHHPPH HHHHHAPPPQ 

      1030       1040       1050       1060       1070       1080 
PHHHHAHPPH PPEMETGGSP DDPPPRLALG PQPSLRGWRG GGPSPTSGAP SPSHHSSSGG 

      1090       1100       1110       1120       1130       1140 
SSGPTQAPAL RYFQLPPRAA SAAMYVPARS GRGRKGPLVK QTKVEGEPQK GSIPSASSPT 

      1150       1160       1170       1180       1190       1200 
SPALPRSEPP PAGPSEKNSI PIPTIIIKAP STSSSGRSSQ GSSTEAEPPT QPDGAGGGGS 

      1210       1220       1230       1240       1250       1260 
SPSPAPATSP VPPSPSPVPT PASPSGPATL DFTSQFGAAL VGAARREGGW QNEARRRSTL 

      1270       1280       1290       1300       1310       1320 
FLSTDAGDED GGDSGLGPGG PPGPRLRHSK SIDEGMFSAE PYLRLESGGS SGGYGAYAAG 

      1330       1340       1350       1360       1370       1380 
SRAYGGSGSS SAFTSFLPPR PLVHPLTGKA LDPASPLGLA LAARERALKE SSEGGGTPQP 

      1390       1400       1410       1420       1430       1440 
PPRPPSPRYD APPPTLHHHS PHSPHSPHAR HEPVLRLWGD PARRELGYRA GLGSQEKALT 

      1450       1460       1470       1480       1490       1500 
ASPPAARRSL LHRLPPTAPG VGPLLLQLGP EPPTPHPGVS KAWRTAAPEE PERLPLHVRF 

      1510       1520       1530       1540       1550       1560 
LENCQARPPP AGTRGSSTED GPGVPPPSPR RVLPTSPTSP RGNEENGLPL LVLPPPAPSV 

      1570       1580       1590       1600       1610       1620 
DVDDGEFLFA EPLPPPLEFS NSFEKPESPL TPGPPHPLPD PPSPATPLPA APPPAVAAAP 

      1630       1640       1650       1660       1670       1680 
PTLDSTASSL TSYDSEVATL TQGAPAAPGD PPAPGPPAPA APAPPAPQPG PDPPPGTDSG 

      1690       1700       1710       1720       1730       1740 
IEEVDSRSSS DHPLETISSA STLSSLSAEG GGNTGGVAGG GAGVASGTEL LDTYVAYLDG 

      1750       1760       1770       1780       1790       1800 
QAFGGSGTPG PPYPPQLMTP SKLRGRALGT SGNLRPGPSG GLRDPVTPTS PTVSVTGAGT 

      1810       1820       1830       1840       1850       1860 
DGLLALSACP GPSTAGVAGG PVAVEPEVPP VPLPAASSLP RKLLPWEEGP GPPPPPLPGP 

      1870       1880       1890       1900       1910       1920 
LSQPQASALA TVKASIISEL SSKLQQFGGS STAGGALPWA RGGSGGSTDS HHGGASYIPE 

      1930       1940       1950       1960       1970       1980 
RTSSLQRQRL SEDSQTSLLS KPSSSIFQNW PKPPLPPLPT GSGVSSSTAA APGATSPSAS 

      1990       2000       2010       2020       2030       2040 
SASASTRHLQ GVEFEMRPPL LRRAPSPSLL PASDHKVSPA PRPSSLPILP SGPIYPGLFD 

      2050       2060       2070       2080       2090       2100 
IRSSPTGGAG GSTDPFAPVF VPPHPGISGG LGGALSGASR SLSPTRLLSL PPDKPFGAKP 

      2110       2120       2130       2140       2150       2160 
LGFWTKFDVA DWLEWLGLSE HRAQFLDHEI DGSHLPALTK EDYVDLGVTR VGHRMNIDRA 


LKFFLER 

« Hide

Isoform 2 [UniParc].

Checksum: B9B7E6A33E26DE48
Show »

FASTA1,553159,899
Isoform 3 [UniParc].

Checksum: BF18578E26D6578C
Show »

FASTA2,158225,477
Isoform 4 (A) [UniParc].

Checksum: 912C1737EC330CB1
Show »

FASTA2,159225,368
Isoform 5 [UniParc].

Checksum: D290DD45558B73AF
Show »

FASTA1,943202,919

References

[1]"Synamon, a novel neuronal protein interacting with synapse-associated protein 90/postsynaptic density-95-associated protein."
Yao I., Hata Y., Hirao K., Deguchi M., Ide N., Takeuchi M., Takai Y.
J. Biol. Chem. 274:27463-27466(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH DLGAP1 AND DLG4.
Tissue: Brain.
[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 4), INTERACTION WITH DLGAP1.
Strain: Sprague-Dawley.
[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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Characterization of the shank family of synaptic proteins. Multiple genes, alternative splicing, and differential expression in brain and development."
Lim S., Naisbitt S., Yoon J., Hwang J.-I., Suh P.-G., Sheng M., Kim E.
J. Biol. Chem. 274:29510-29518(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3; 4 AND 5), DEVELOPMENTAL STAGE.
Tissue: Brain.
[5]"Somatostatin receptor interacting protein defines a novel family of multidomain proteins present in human and rodent brain."
Zitzer H., Hoenck H.-H., Baechner D., Richter D., Kreienkamp H.-J.
J. Biol. Chem. 274:32997-33001(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4).
Tissue: Brain.
[6]"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, SUBCELLULAR LOCATION.
[7]"Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin."
Bockers T.M., Mameza M.G., Kreutz M.R., Bockmann J., Weise C., Buck F., Richter D., Gundelfinger E.D., Kreienkamp H.-J.
J. Biol. Chem. 276:40104-40112(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPTAN1.
[8]"Sharpin, a novel postsynaptic density protein that directly interacts with the shank family of proteins."
Lim S., Sala C., Yoon J., Park S., Kuroda S., Sheng M., Kim E.
Mol. Cell. Neurosci. 17:385-397(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHARPIN.
[9]"Regulation of dendritic spine morphology and synaptic function by Shank and Homer."
Sala C., Piech V., Wilson N.R., Passafaro M., Liu G., Sheng M.
Neuron 31:115-130(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The Shank family of scaffold proteins."
Sheng M., Kim E.
J. Cell Sci. 113:1851-1856(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"The immunoglobulin family member dendrite arborization and synapse maturation 1 (Dasm1) controls excitatory synapse maturation."
Shi S.-H., Cheng T., Jan L.Y., Jan Y.-N.
Proc. Natl. Acad. Sci. U.S.A. 101:13346-13351(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGSF9.
[12]"Paralemmin-1, a modulator of filopodia induction is required for spine maturation."
Arstikaitis P., Gauthier-Campbell C., Carolina Gutierrez Herrera R., Huang K., Levinson J.N., Murphy T.H., Kilimann M.W., Sala C., Colicos M.A., El-Husseini A.
Mol. Biol. Cell 19:2026-2038(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization."
Im Y.J., Lee J.H., Park S.H., Park S.J., Rho S.-H., Kang G.B., Kim E., Eom S.H.
J. Biol. Chem. 278:48099-48104(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 654-762 IN COMPLEX WITH DLGAP1, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF102855 mRNA. Translation: AAD04569.2.
AF131951 mRNA. Translation: AAD29417.1. Different initiation.
AF159046 mRNA. Translation: AAD42975.1.
AF141904 mRNA. Translation: AAF02498.1. Different initiation.
RefSeqNP_113939.2. NM_031751.2. [Q9WV48-1]
XP_006229214.1. XM_006229152.1. [Q9WV48-4]
XP_006229215.1. XM_006229153.1. [Q9WV48-3]
XP_006229219.1. XM_006229157.1. [Q9WV48-5]
UniGeneRn.225968.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q3OX-ray1.80A/B654-762[»]
1Q3PX-ray2.25A/B654-762[»]
3L4FX-ray2.80D653-765[»]
3QJMX-ray2.31A/B654-768[»]
3QJNX-ray2.71A/B/C/D/E/F/G/H654-768[»]
ProteinModelPortalQ9WV48.
SMRQ9WV48. Positions 656-759, 2101-2162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249365. 5 interactions.
IntActQ9WV48. 17 interactions.
MINTMINT-101286.

PTM databases

PhosphoSiteQ9WV48.

Proteomic databases

PaxDbQ9WV48.
PRIDEQ9WV48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026100; ENSRNOP00000026100; ENSRNOG00000019207. [Q9WV48-1]
ENSRNOT00000044257; ENSRNOP00000039860; ENSRNOG00000019207. [Q9WV48-3]
ENSRNOT00000048805; ENSRNOP00000042890; ENSRNOG00000019207. [Q9WV48-4]
ENSRNOT00000049346; ENSRNOP00000044509; ENSRNOG00000019207. [Q9WV48-5]
GeneID78957.
KEGGrno:78957.
UCSCRGD:621011. rat. [Q9WV48-1]

Organism-specific databases

CTD50944.
RGD621011. Shank1.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00510000046474.
HOGENOMHOG000293276.
HOVERGENHBG079186.
InParanoidQ9WV48.
KOK15009.
OMAWEEGPGP.
OrthoDBEOG7X6KZ7.
PhylomeDBQ9WV48.

Gene expression databases

GenevestigatorQ9WV48.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
1.25.40.20. 1 hit.
2.30.42.10. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF12796. Ank_2. 2 hits.
PF00595. PDZ. 1 hit.
PF00536. SAM_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 6 hits.
SM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS50106. PDZ. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9WV48.
NextBio614372.
PROQ9WV48.

Entry information

Entry nameSHAN1_RAT
AccessionPrimary (citable) accession number: Q9WV48
Secondary accession number(s): Q9QZZ8, Q9WU13, Q9WUE8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: November 1, 1999
Last modified: June 11, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references