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Q80Z38 (SHAN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. 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·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 2

Short name=Shank2
Alternative name(s):
Cortactin-binding protein 1
Short name=CortBP1
Gene names
Name:Shank2
Synonyms:Cortbp1, Kiaa1022
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1476 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. May play a role in the structural and functional organization of the dendritic spine and synaptic junction By similarity.

Subunit structure

Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP. Interacts with CTTN/cortactin SH3 domain, DLGAP1/GKAP and alpha-latrotoxin receptor 1. Interacts with DNM2, DBNL, GRID2, BAIAP2, SLC9A3, PLCB3 and CFTR. Interacts (via proline-rich region) with PDE4D. Interacts with ABI1 (via SH3 domain). Ref.1 Ref.9

Subcellular location

Apical cell membrane By similarity. Cytoplasm. Cell junctionsynapse. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell projectiondendritic spine. Cell projectiongrowth cone By similarity. Note: Colocalizes with cortactin in growth cones in differentiating hippocampal neurons. Colocalized with PDE4D to the apical membrane of colonic crypt cells By similarity. Present in the dendritic spines of cerebellar Purkinje cells. Ref.1

Tissue specificity

Detected in brain (at protein level), where it is highly expressed in Purkinje cells. Ref.6 Ref.9 Ref.10

Domain

The PDZ domain is required for interaction with GRID2, PLCB3, SLC9A3 and CFTR.

Disruption phenotype

Mutants are viable, but with reduced body weight and a lower survival rate compared to their wild-type littermates. They are extremely hiperactive and display profound autistic-like behavioral alterations including repetitive grooming as well as abnormalities in vocal and social behaviors. Mutants exhibit fewer dendritic spines and show reduced basal synaptic transmission, a reduced frequency of miniature excitatory postsynaptic currents and enhanced NMDA receptor-mediated excitatory currents at the physiological level. They also show a brain-region-specific up-regulation of ionotropic glutamate receptors and increased levels of SHANK3. Ref.11

Sequence similarities

Belongs to the SHANK family.

Contains 1 PDZ (DHR) domain.

Contains 1 SAM (sterile alpha motif) domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainSH3 domain
SH3-binding
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult behavior

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

exploration behavior

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

learning

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

long term synaptic depression

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

long-term synaptic potentiation

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

memory

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

social behavior

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

synapse assembly

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

vocalization behavior

Inferred from mutant phenotype PubMed 22699620. Source: BHF-UCL

   Cellular_componentapical plasma membrane

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

brush border membrane

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

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

ciliary membrane

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

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendritic spine

Inferred from direct assay Ref.1. Source: BHF-UCL

growth cone

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

neuron projection

Inferred from direct assay PubMed 21795692. Source: BHF-UCL

neuronal cell body

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

photoreceptor inner segment

Inferred from direct assay PubMed 19299912. Source: BHF-UCL

photoreceptor outer segment

Inferred from direct assay PubMed 19299912. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.1. Source: BHF-UCL

postsynaptic density

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

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionionotropic glutamate receptor binding

Inferred from physical interaction Ref.1PubMed 16606358. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80Z38-1)

Also known as: E;

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: Q80Z38-2)

The sequence of this isoform differs from the canonical sequence as follows:
     380-383: Missing.
Isoform 3 (identifier: Q80Z38-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-210: Missing.
     211-238: SQAETRADRSKKLFRHYTVGSYDSFDAA → MMSVPGGGAATVMMTGYNNGRYPRNSLY
     380-383: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14761476SH3 and multiple ankyrin repeat domains protein 2
PRO_0000247760

Regions

Domain147 – 20660SH3
Domain247 – 34195PDZ
Domain1413 – 147664SAM
Motif1169 – 11757SH3-binding Potential
Compositional bias24 – 274Poly-Arg
Compositional bias355 – 3584Poly-Pro
Compositional bias513 – 56048Pro-rich
Compositional bias1017 – 10204Poly-Pro
Compositional bias1169 – 121143Pro-rich
Compositional bias1348 – 13536Poly-Pro

Amino acid modifications

Modified residue5861Phosphoserine Ref.7
Modified residue9031Phosphothreonine Ref.7
Glycosylation12921O-linked (GlcNAc) Ref.8

Natural variations

Alternative sequence1 – 210210Missing in isoform 3.
VSP_041614
Alternative sequence211 – 23828SQAET…SFDAA → MMSVPGGGAATVMMTGYNNG RYPRNSLY in isoform 3.
VSP_041615
Alternative sequence380 – 3834Missing in isoform 2 and isoform 3.
VSP_020040

Experimental info

Sequence conflict10711S → P in BAC58120. Ref.1
Sequence conflict10711S → P in BAD90424. Ref.5

Sequences

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

Last modified July 27, 2011. Version 2.
Checksum: 0B5B0EBDFD6BAAA7

FASTA1,476158,969
        10         20         30         40         50         60 
MKSLLNAFTK KEVPFREAPA YSNRRRRPPN TLAAPRVLLR SNSDNNLNAG APEWAVCSAA 

        70         80         90        100        110        120 
TSHRSLSPQL LQQTPSKPDG ATKSLGSYTP GPRSRSPSLN RLGGTAEDGK RTQPHWHVGS 

       130        140        150        160        170        180 
PFTPGANKDS LSTFEYPGPR RKLYSAVPGR LFVAVKPYQP QVDGEIPLHR GDRVKVLSIG 

       190        200        210        220        230        240 
EGGFWEGSAR GHIGWFPAEC VEEVQCKPRD SQAETRADRS KKLFRHYTVG SYDSFDAASD 

       250        260        270        280        290        300 
CIIEDKTVVL QKKDNEGFGF VLRGAKADTP IEEFTPTPAF PALQYLESVD EGGVAWQAGL 

       310        320        330        340        350        360 
RTGDFLIEVN NENVVKVGHR QVVNMIRQGG NHLILKVVTV TRNLDPDDTA RKKAPPPPKR 

       370        380        390        400        410        420 
APTTALTLRS KSMTAELEEL GLSLVDKASV RKKKDKPEEI VPASKPSRTA ENVAIESRVA 

       430        440        450        460        470        480 
TIKQRPTSRC FPAASDVNSV YERQGIAVMT PTVPGSPKGP FLGLPRGTMR RQKSIDSRIF 

       490        500        510        520        530        540 
LSGITEEERQ FLAPPMLKFT RSLSMPDTSE DIPPPPQSVP PSPPPPSPTT YNCPRSPTPR 

       550        560        570        580        590        600 
VYGTIKPAFN QNPVVAKVPP ATRSDTVATM MREKGMFYRR ELDRFSLDSE DVYSRSPAPQ 

       610        620        630        640        650        660 
AAFRTKRGQM PENPYSEVGK IASKAVYVPA KPARRKGVLV KQSNVEDSPE KTCSIPIPTI 

       670        680        690        700        710        720 
IVKEPSTSSS GKSSQGSSME IDPQATEPGQ LRPDDSLTVS SPFAAAIAGA VRDREKRLEA 

       730        740        750        760        770        780 
RRNSPAFLST DLGDEDVGLG PPAPRMQASK FPEEGGFGDE DETEQPLLPT PGAAPRELEN 

       790        800        810        820        830        840 
HFLGGGEAGA QGEAGGPLSS TSKAKGPESG PAAPLKSSSP AGPENYVHPL TGRLLDPSSP 

       850        860        870        880        890        900 
LALALSARDR AMQESQQGHK GEAPKADLNK PLYIDTKMRP SVESGFPPVT RQNTRGPLRR 

       910        920        930        940        950        960 
QETENKYETD LGKDRRADDK KNMLINIVDT AQQKSAGLLM VHTVDVPMAG PPLEEEEDRE 

       970        980        990       1000       1010       1020 
DGDTKPDHSP STVPEGVPKT EGALQISAAP EPAVAPGRTI VAAGSVEEAV ILPFRIPPPP 

      1030       1040       1050       1060       1070       1080 
LASVDLDEDF LFTEPLPPPL EFANSFDIPD DRAASVPALA DLVKQKKNDT SQPPTLNSSQ 

      1090       1100       1110       1120       1130       1140 
PANSTDSKKP AGISNCLPSS FLPPPESFDA VTDSGIEEVD SRSSSDHHLE TTSTISTVSS 

      1150       1160       1170       1180       1190       1200 
ISTLSSEGGE SMDTCTVYAD GQAFVVDKPP VPPKPKMKPI VHKSNALYQD TLPEEDTDGF 

      1210       1220       1230       1240       1250       1260 
VIPPPAPPPP PGSAQAGVAK VIQPRTSKLW GDVPEVKSPI LSGPKANVIS ELNSILQQMN 

      1270       1280       1290       1300       1310       1320 
RGKSVKPGEG LELPVGAKSA NLAPRSPEVM STVSGTRSTT VTFTVRPGTS QPITLQSRPP 

      1330       1340       1350       1360       1370       1380 
DYESRTSGPR RAPSPVVSPT ELSKEILPTP PPPSATAASP SPTLSDVFSL PSQSPAGDLF 

      1390       1400       1410       1420       1430       1440 
GLNPAGRSRS PSPSILQQPI SNKPFTTKPV HLWTKPDVAD WLESLNLGEH KETFMDNEID 

      1450       1460       1470 
GSHLPNLQKE DLIDLGVTRV GHRMNIERAL KQLLDR 

« Hide

Isoform 2 [UniParc].

Checksum: 0BBCF1E8E351834C
Show »

FASTA1,472158,599
Isoform 3 [UniParc].

Checksum: BF3B96EFA165D7B9
Show »

FASTA1,262135,412

References

« Hide 'large scale' references
[1]"Direct interaction of GluRdelta2 with Shank scaffold proteins in cerebellar Purkinje cells."
Uemura T., Mori H., Mishina M.
Mol. Cell. Neurosci. 26:330-341(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH GRID2.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-350 (ISOFORMS 1/2).
Strain: C57BL/6J.
Tissue: Brain cortex.
[5]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-1476 (ISOFORM 2).
Tissue: Fetal brain.
[6]"Identification of a novel cortactin SH3 domain-binding protein and its localization to growth cones of cultured neurons."
Du Y., Weed S.A., Xiong W.-C., Marshall T.D., Parsons J.T.
Mol. Cell. Biol. 18:5838-5851(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586 AND THR-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry."
Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-1292.
Tissue: Brain.
[9]"Dynamic regulation of cystic fibrosis transmembrane conductance regulator by competitive interactions of molecular adaptors."
Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M., Lee M.G.
J. Biol. Chem. 282:10414-10422(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDE4D, TISSUE SPECIFICITY.
[10]"Shank3 mutant mice display autistic-like behaviours and striatal dysfunction."
Peca J., Feliciano C., Ting J.T., Wang W., Wells M.F., Venkatraman T.N., Lascola C.D., Fu Z., Feng G.
Nature 472:437-442(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Autistic-like behaviours and hyperactivity in mice lacking ProSAP1/Shank2."
Schmeisser M.J., Ey E., Wegener S., Bockmann J., Stempel A.V., Kuebler A., Janssen A.L., Udvardi P.T., Shiban E., Spilker C., Balschun D., Skryabin B.V., Dieck S.T., Smalla K.H., Montag D., Leblond C.S., Faure P., Torquet N. expand/collapse author list , Le Sourd A.M., Toro R., Grabrucker A.M., Shoichet S.A., Schmitz D., Kreutz M.R., Bourgeron T., Gundelfinger E.D., Boeckers T.M.
Nature 486:256-260(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB099695 mRNA. Translation: BAC58120.1.
AC124520 Genomic DNA. No translation available.
AC127546 Genomic DNA. No translation available.
AC140268 Genomic DNA. No translation available.
AC152166 Genomic DNA. No translation available.
BC167171 mRNA. Translation: AAI67171.1.
AK139360 mRNA. Translation: BAE23976.1.
AK220363 mRNA. Translation: BAD90424.1.
CCDSCCDS40201.1. [Q80Z38-3]
RefSeqNP_001074839.2. NM_001081370.2.
NP_001106844.2. NM_001113373.2.
XP_006508596.1. XM_006508533.1. [Q80Z38-1]
UniGeneMm.483624.

3D structure databases

ProteinModelPortalQ80Z38.
SMRQ80Z38. Positions 148-205, 240-343, 1410-1473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229144. 2 interactions.
IntActQ80Z38. 4 interactions.

PTM databases

PhosphoSiteQ80Z38.

Proteomic databases

MaxQBQ80Z38.
PaxDbQ80Z38.
PRIDEQ80Z38.

Protocols and materials databases

DNASU210274.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097929; ENSMUSP00000095542; ENSMUSG00000037541. [Q80Z38-3]
GeneID210274.
KEGGmmu:210274.
UCSCuc009kqe.2. mouse. [Q80Z38-2]
uc009kqf.1. mouse. [Q80Z38-3]
uc009kqg.1. mouse. [Q80Z38-1]

Organism-specific databases

CTD22941.
MGIMGI:2671987. Shank2.
RougeSearch...

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00510000046474.
HOGENOMHOG000293276.
HOVERGENHBG054027.
KOK15009.

Gene expression databases

BgeeQ80Z38.
CleanExMM_SHANK2.
GenevestigatorQ80Z38.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.30.42.10. 1 hit.
InterProIPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00595. PDZ. 1 hit.
PF00536. SAM_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTSM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEPS50106. PDZ. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio372912.
PROQ80Z38.
SOURCESearch...

Entry information

Entry nameSHAN2_MOUSE
AccessionPrimary (citable) accession number: Q80Z38
Secondary accession number(s): E9QPH7, Q3UTK4, Q5DU07
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 87 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot