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O43815 (STRN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Striatin
Gene names
Name:STRN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calmodulin-binding protein which may function as scaffolding or signaling protein and may play a role in dendritic Ca2+ signaling.

Subunit structure

Interacts with protein phosphatase 2A (PP2A) Potential. Interacts with CTTNBP2; this interaction may regulate dendritic spine distribution of STRN. Activation of glutamate receptors weakens the interaction with CTTNBP2 By similarity.

Subcellular location

Cytoplasm By similarity. Membrane; Peripheral membrane protein By similarity. Cell projectiondendritic spine By similarity. Note: CTTNBP2-binding may regulate dendritic spine distribution By similarity.

Tissue specificity

Preferentially expressed in brain. Ref.1

Sequence similarities

Belongs to the WD repeat striatin family.

Contains 6 WD repeats.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
WD repeat
   LigandCalmodulin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from mutant phenotype PubMed 18502210. Source: UniProtKB

dendrite development

Inferred from sequence or structural similarity. Source: UniProtKB

locomotory behavior

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 18502210. Source: UniProtKB

tight junction assembly

Non-traceable author statement PubMed 18502210. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

dendritic spine

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from sequence or structural similarity. Source: UniProtKB

tight junction

Inferred from direct assay PubMed 18502210. Source: UniProtKB

   Molecular_functionarmadillo repeat domain binding

Inferred from physical interaction PubMed 18502210. Source: UniProtKB

calmodulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

estrogen receptor binding

Inferred from physical interaction PubMed 15569929. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17540176PubMed 18782753PubMed 22153077PubMed 23455922PubMed 24255178PubMed 24366813. Source: IntAct

protein complex binding

Inferred from direct assay PubMed 18782753. Source: UniProtKB

protein phosphatase 2A binding

Inferred from direct assay PubMed 18782753. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43815-1)

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: O43815-2)

The sequence of this isoform differs from the canonical sequence as follows:
     29-40: Missing.
     311-348: EKEDQCLMPEAWNVDQGVITKLKEQYKKERKGKKGVKR → G
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 780780Striatin
PRO_0000051232

Regions

Repeat461 – 50040WD 1
Repeat514 – 55340WD 2
Repeat567 – 60640WD 3
Repeat662 – 70140WD 4
Repeat704 – 74340WD 5
Repeat750 – 77930WD 6
Region55 – 639Caveolin-binding Potential
Region149 – 16618Calmodulin-binding Potential
Coiled coil53 – 12068 Potential

Amino acid modifications

Modified residue2451Phosphoserine Ref.4 Ref.6 Ref.7

Natural variations

Alternative sequence29 – 4012Missing in isoform 2.
VSP_023495
Alternative sequence311 – 34838EKEDQ…KGVKR → G in isoform 2.
VSP_023496

Experimental info

Sequence conflict1911S → I in CAA11560. Ref.1
Sequence conflict4231L → P in CAA11560. Ref.1
Sequence conflict6111T → I in CAA11560. Ref.1
Sequence conflict6771P → S in CAA11560. Ref.1

Sequences

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

Last modified March 6, 2007. Version 4.
Checksum: DDB18A11102BEA35

FASTA78086,132
        10         20         30         40         50         60 
MDEQAGPGVF FSNNHPGAGG AKGLGPLAEA AAAGDGAAAA GAARAQYSLP GILHFLQHEW 

        70         80         90        100        110        120 
ARFEVERAQW EVERAELQAQ IAFLQGERKG QENLKKDLVR RIKMLEYALK QERAKYHKLK 

       130        140        150        160        170        180 
YGTELNQGDM KPPSYDSDEG NETEVQPQQN SQLMWKQGRQ LLRQYLQEVG YTDTILDVKS 

       190        200        210        220        230        240 
KRVRALLGFS SDVTDREDDK NQDSVVNGTE AEVKETAMIA KSELTDSASV LDNFKFLESA 

       250        260        270        280        290        300 
AADFSDEDED DDVDGREKSV IDTSTIVRKK ALPDSGEDRD TKEALKEFDF LVTSEEGDNE 

       310        320        330        340        350        360 
SRSAGDGTDW EKEDQCLMPE AWNVDQGVIT KLKEQYKKER KGKKGVKRPN RSKLQDMLAN 

       370        380        390        400        410        420 
LRDVDELPSL QPSVGSPSRP SSSRLPEHEI NRADEVEALT FPPSSGKSFI MGADEALESE 

       430        440        450        460        470        480 
LGLGELAGLT VANEADSLTY DIANNKDALR KTWNPKFTLR SHFDGIRALA FHPIEPVLIT 

       490        500        510        520        530        540 
ASEDHTLKMW NLQKTAPAKK STSLDVEPIY TFRAHKGPVL CVVMSSNGEQ CYSGGTDGLI 

       550        560        570        580        590        600 
QGWNTTNPNI DPYDSYDPSV LRGPLLGHTD AVWGLAYSAA HQRLLSCSAD GTLRLWNTTE 

       610        620        630        640        650        660 
VAPALSVFND TKELGIPASV DLVSSDPSHM VASFSKGYTS IFNMETQQRI LTLESNVDTT 

       670        680        690        700        710        720 
ANSSCQINRV ISHPTLPISI TAHEDRHIKF YDNNTGKLIH SMVAHLEAVT SLAVDPNGLY 

       730        740        750        760        770        780 
LMSGSHDCSI RLWNLESKTC IQEFTAHRKK FEESIHDVAF HPSKCYIASA GADALAKVFV 

« Hide

Isoform 2 [UniParc].

Checksum: 67B5DD94E3499AB7
Show »

FASTA73180,761

References

« Hide 'large scale' references
[1]"Cloning of human striatin cDNA (STRN), gene mapping to 2p22-p21, and preferential expression in brain."
Moqrich A., Mattei M.-G., Bartoli M., Rakitina T., Baillat G., Monneron A., Castets F.
Genomics 51:136-139(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 2).
[4]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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 SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ223814 mRNA. Translation: CAA11560.1.
AC007404 Genomic DNA. Translation: AAY24273.1.
AC007382 Genomic DNA. Translation: AAF66162.1.
BC106879 mRNA. Translation: AAI06880.1.
CCDSCCDS1784.1. [O43815-1]
RefSeqNP_003153.2. NM_003162.3. [O43815-1]
UniGeneHs.127486.

3D structure databases

ProteinModelPortalO43815.
SMRO43815. Positions 70-114, 401-779.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112674. 46 interactions.
IntActO43815. 37 interactions.
MINTMINT-2796380.
STRING9606.ENSP00000263918.

PTM databases

PhosphoSiteO43815.

Proteomic databases

MaxQBO43815.
PaxDbO43815.
PRIDEO43815.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263918; ENSP00000263918; ENSG00000115808. [O43815-1]
ENST00000379213; ENSP00000368513; ENSG00000115808. [O43815-2]
GeneID6801.
KEGGhsa:6801.
UCSCuc002rpn.3. human. [O43815-1]
uc010ezx.3. human. [O43815-2]

Organism-specific databases

CTD6801.
GeneCardsGC02M036987.
HGNCHGNC:11424. STRN.
HPAHPA017286.
MIM614765. gene.
neXtProtNX_O43815.
PharmGKBPA36224.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000236343.
HOVERGENHBG007117.
InParanoidO43815.
KOK17608.
OMAGPISEAW.
OrthoDBEOG79KPDR.
PhylomeDBO43815.
TreeFamTF313387.

Enzyme and pathway databases

SignaLinkO43815.

Gene expression databases

BgeeO43815.
CleanExHS_STRN.
GenevestigatorO43815.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR013258. Striatin_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF08232. Striatin. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSTRN.
GenomeRNAi6801.
NextBio26559.
PMAP-CutDBO43815.
PROO43815.
SOURCESearch...

Entry information

Entry nameSTRN_HUMAN
AccessionPrimary (citable) accession number: O43815
Secondary accession number(s): Q3KP65, Q53TQ8, Q9NP38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM