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Q80Z38

- SHAN2_MOUSE

UniProt

Q80Z38 - SHAN2_MOUSE

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Protein
SH3 and multiple ankyrin repeat domains protein 2
Gene
Shank2, Cortbp1, Kiaa1022
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. ionotropic glutamate receptor binding Source: BHF-UCL

GO - Biological processi

  1. adult behavior Source: BHF-UCL
  2. exploration behavior Source: BHF-UCL
  3. learning Source: BHF-UCL
  4. long term synaptic depression Source: BHF-UCL
  5. long-term synaptic potentiation Source: BHF-UCL
  6. memory Source: BHF-UCL
  7. social behavior Source: BHF-UCL
  8. synapse assembly Source: BHF-UCL
  9. vocalization behavior Source: BHF-UCL
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
SH3 and multiple ankyrin repeat domains protein 2
Short name:
Shank2
Alternative name(s):
Cortactin-binding protein 1
Short name:
CortBP1
Gene namesi
Name:Shank2
Synonyms:Cortbp1, Kiaa1022
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:2671987. Shank2.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. apical plasma membrane Source: BHF-UCL
  2. brush border membrane Source: BHF-UCL
  3. cell junction Source: UniProtKB-KW
  4. ciliary membrane Source: BHF-UCL
  5. cytoplasm Source: UniProtKB-SubCell
  6. dendritic spine Source: BHF-UCL
  7. growth cone Source: BHF-UCL
  8. neuron projection Source: BHF-UCL
  9. neuronal cell body Source: BHF-UCL
  10. photoreceptor inner segment Source: BHF-UCL
  11. photoreceptor outer segment Source: BHF-UCL
  12. plasma membrane Source: BHF-UCL
  13. postsynaptic density Source: BHF-UCL
  14. postsynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

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 SHANK3.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14761476SH3 and multiple ankyrin repeat domains protein 2
PRO_0000247760Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei586 – 5861Phosphoserine1 Publication
Modified residuei903 – 9031Phosphothreonine1 Publication
Glycosylationi1292 – 12921O-linked (GlcNAc)1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ80Z38.
PaxDbiQ80Z38.
PRIDEiQ80Z38.

PTM databases

PhosphoSiteiQ80Z38.

Expressioni

Tissue specificityi

Detected in brain (at protein level), where it is highly expressed in Purkinje cells.3 Publications

Gene expression databases

BgeeiQ80Z38.
CleanExiMM_SHANK2.
GenevestigatoriQ80Z38.

Interactioni

Subunit structurei

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).2 Publications

Protein-protein interaction databases

BioGridi229144. 2 interactions.
IntActiQ80Z38. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ80Z38.
SMRiQ80Z38. Positions 148-205, 240-343, 1410-1473.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 20660SH3
Add
BLAST
Domaini247 – 34195PDZ
Add
BLAST
Domaini1413 – 147664SAM
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1169 – 11757SH3-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi24 – 274Poly-Arg
Compositional biasi355 – 3584Poly-Pro
Compositional biasi513 – 56048Pro-rich
Add
BLAST
Compositional biasi1017 – 10204Poly-Pro
Compositional biasi1169 – 121143Pro-rich
Add
BLAST
Compositional biasi1348 – 13536Poly-Pro

Domaini

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

Sequence similaritiesi

Belongs to the SHANK family.
Contains 1 PDZ (DHR) domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00510000046474.
HOGENOMiHOG000293276.
HOVERGENiHBG054027.
KOiK15009.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00595. PDZ. 1 hit.
PF00536. SAM_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q80Z38-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MKSLLNAFTK KEVPFREAPA YSNRRRRPPN TLAAPRVLLR SNSDNNLNAG     50
APEWAVCSAA TSHRSLSPQL LQQTPSKPDG ATKSLGSYTP GPRSRSPSLN 100
RLGGTAEDGK RTQPHWHVGS PFTPGANKDS LSTFEYPGPR RKLYSAVPGR 150
LFVAVKPYQP QVDGEIPLHR GDRVKVLSIG EGGFWEGSAR GHIGWFPAEC 200
VEEVQCKPRD SQAETRADRS KKLFRHYTVG SYDSFDAASD CIIEDKTVVL 250
QKKDNEGFGF VLRGAKADTP IEEFTPTPAF PALQYLESVD EGGVAWQAGL 300
RTGDFLIEVN NENVVKVGHR QVVNMIRQGG NHLILKVVTV TRNLDPDDTA 350
RKKAPPPPKR APTTALTLRS KSMTAELEEL GLSLVDKASV RKKKDKPEEI 400
VPASKPSRTA ENVAIESRVA TIKQRPTSRC FPAASDVNSV YERQGIAVMT 450
PTVPGSPKGP FLGLPRGTMR RQKSIDSRIF LSGITEEERQ FLAPPMLKFT 500
RSLSMPDTSE DIPPPPQSVP PSPPPPSPTT YNCPRSPTPR VYGTIKPAFN 550
QNPVVAKVPP ATRSDTVATM MREKGMFYRR ELDRFSLDSE DVYSRSPAPQ 600
AAFRTKRGQM PENPYSEVGK IASKAVYVPA KPARRKGVLV KQSNVEDSPE 650
KTCSIPIPTI IVKEPSTSSS GKSSQGSSME IDPQATEPGQ LRPDDSLTVS 700
SPFAAAIAGA VRDREKRLEA RRNSPAFLST DLGDEDVGLG PPAPRMQASK 750
FPEEGGFGDE DETEQPLLPT PGAAPRELEN HFLGGGEAGA QGEAGGPLSS 800
TSKAKGPESG PAAPLKSSSP AGPENYVHPL TGRLLDPSSP LALALSARDR 850
AMQESQQGHK GEAPKADLNK PLYIDTKMRP SVESGFPPVT RQNTRGPLRR 900
QETENKYETD LGKDRRADDK KNMLINIVDT AQQKSAGLLM VHTVDVPMAG 950
PPLEEEEDRE DGDTKPDHSP STVPEGVPKT EGALQISAAP EPAVAPGRTI 1000
VAAGSVEEAV ILPFRIPPPP LASVDLDEDF LFTEPLPPPL EFANSFDIPD 1050
DRAASVPALA DLVKQKKNDT SQPPTLNSSQ PANSTDSKKP AGISNCLPSS 1100
FLPPPESFDA VTDSGIEEVD SRSSSDHHLE TTSTISTVSS ISTLSSEGGE 1150
SMDTCTVYAD GQAFVVDKPP VPPKPKMKPI VHKSNALYQD TLPEEDTDGF 1200
VIPPPAPPPP PGSAQAGVAK VIQPRTSKLW GDVPEVKSPI LSGPKANVIS 1250
ELNSILQQMN RGKSVKPGEG LELPVGAKSA NLAPRSPEVM STVSGTRSTT 1300
VTFTVRPGTS QPITLQSRPP DYESRTSGPR RAPSPVVSPT ELSKEILPTP 1350
PPPSATAASP SPTLSDVFSL PSQSPAGDLF GLNPAGRSRS PSPSILQQPI 1400
SNKPFTTKPV HLWTKPDVAD WLESLNLGEH KETFMDNEID GSHLPNLQKE 1450
DLIDLGVTRV GHRMNIERAL KQLLDR 1476
Length:1,476
Mass (Da):158,969
Last modified:July 27, 2011 - v2
Checksum:i0B5B0EBDFD6BAAA7
GO
Isoform 2 (identifier: Q80Z38-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     380-383: Missing.

Show »
Length:1,472
Mass (Da):158,599
Checksum:i0BBCF1E8E351834C
GO
Isoform 3 (identifier: Q80Z38-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,262
Mass (Da):135,412
Checksum:iBF3B96EFA165D7B9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 210210Missing in isoform 3.
VSP_041614Add
BLAST
Alternative sequencei211 – 23828SQAET…SFDAA → MMSVPGGGAATVMMTGYNNG RYPRNSLY in isoform 3.
VSP_041615Add
BLAST
Alternative sequencei380 – 3834Missing in isoform 2 and isoform 3.
VSP_020040

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1071 – 10711S → P in BAC58120. 1 Publication
Sequence conflicti1071 – 10711S → P in BAD90424. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS40201.1. [Q80Z38-3]
RefSeqiNP_001074839.2. NM_001081370.2.
NP_001106844.2. NM_001113373.2.
XP_006508596.1. XM_006508533.1. [Q80Z38-1]
UniGeneiMm.483624.

Genome annotation databases

EnsembliENSMUST00000097929; ENSMUSP00000095542; ENSMUSG00000037541. [Q80Z38-3]
GeneIDi210274.
KEGGimmu:210274.
UCSCiuc009kqe.2. mouse. [Q80Z38-2]
uc009kqf.1. mouse. [Q80Z38-3]
uc009kqg.1. mouse. [Q80Z38-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS40201.1. [Q80Z38-3 ]
RefSeqi NP_001074839.2. NM_001081370.2.
NP_001106844.2. NM_001113373.2.
XP_006508596.1. XM_006508533.1. [Q80Z38-1 ]
UniGenei Mm.483624.

3D structure databases

ProteinModelPortali Q80Z38.
SMRi Q80Z38. Positions 148-205, 240-343, 1410-1473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229144. 2 interactions.
IntActi Q80Z38. 4 interactions.

PTM databases

PhosphoSitei Q80Z38.

Proteomic databases

MaxQBi Q80Z38.
PaxDbi Q80Z38.
PRIDEi Q80Z38.

Protocols and materials databases

DNASUi 210274.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000097929 ; ENSMUSP00000095542 ; ENSMUSG00000037541 . [Q80Z38-3 ]
GeneIDi 210274.
KEGGi mmu:210274.
UCSCi uc009kqe.2. mouse. [Q80Z38-2 ]
uc009kqf.1. mouse. [Q80Z38-3 ]
uc009kqg.1. mouse. [Q80Z38-1 ]

Organism-specific databases

CTDi 22941.
MGIi MGI:2671987. Shank2.
Rougei Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00510000046474.
HOGENOMi HOG000293276.
HOVERGENi HBG054027.
KOi K15009.

Miscellaneous databases

NextBioi 372912.
PROi Q80Z38.
SOURCEi Search...

Gene expression databases

Bgeei Q80Z38.
CleanExi MM_SHANK2.
Genevestigatori Q80Z38.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.30.42.10. 1 hit.
InterProi IPR001478. PDZ.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF00595. PDZ. 1 hit.
PF00536. SAM_1. 1 hit.
PF07653. SH3_2. 1 hit.
[Graphical view ]
SMARTi SM00228. PDZ. 1 hit.
SM00454. SAM. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 1 hit.
PROSITEi PS50106. PDZ. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSHAN2_MOUSE
AccessioniPrimary (citable) accession number: Q80Z38
Secondary accession number(s): E9QPH7, Q3UTK4, Q5DU07
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi