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Q9NRL3 (STRN4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Striatin-4
Alternative name(s):
Zinedin
Gene names
Name:STRN4
Synonyms:ZIN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds calmodulin in a calcium dependent manner. May function as scaffolding or signaling protein.

Subunit structure

Interacts with CTTNBP2; this interaction may regulate dendritic spine distribution of STRN4. Activation of glutamate receptors weakens the interaction with CTTNBP2 By similarity. Interacts with CTTNBP2NL. Ref.6

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.

Miscellaneous

The name 'Zinedin' probably originates from the name of the famous soccer player from Marseille (Zinedine Zidane).

Sequence similarities

Belongs to the WD repeat striatin family.

Contains 7 WD repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

JUNP054123EBI-717245,EBI-852823

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 753753Striatin-4
PRO_0000051239

Regions

Repeat436 – 47540WD 1
Repeat489 – 52840WD 2
Repeat542 – 58140WD 3
Repeat587 – 62842WD 4
Repeat635 – 67440WD 5
Repeat677 – 71640WD 6
Repeat723 – 75230WD 7
Region71 – 799Caveolin-binding Potential
Region165 – 18218Calmodulin-binding Potential
Coiled coil69 – 13668 Potential
Compositional bias6 – 149Poly-Ala

Amino acid modifications

Modified residue531Phosphoserine Ref.8 Ref.10
Modified residue2061Phosphoserine Ref.7 Ref.8
Modified residue2761Phosphoserine Ref.4

Natural variations

Natural variant5681V → I.
Corresponds to variant rs10409124 [ dbSNP | Ensembl ].
VAR_053419

Experimental info

Sequence conflict3561I → V in AAF29527. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NRL3 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 339AC24E26A9CD54

FASTA75380,596
        10         20         30         40         50         60 
MMEERAAAAV AAAASSCRPL GSGAGPGPTG AAPVSAPAPG PGPAGKGGGG GGSPGPTAGP 

        70         80         90        100        110        120 
EPLSLPGILH FIQHEWARFE AEKARWEAER AELQAQVAFL QGERKGQENL KTDLVRRIKM 

       130        140        150        160        170        180 
LEYALKQERA KYHKLKFGTD LNQGEKKADV SEQVSNGPVE SVTLENSPLV WKEGRQLLRQ 

       190        200        210        220        230        240 
YLEEVGYTDT ILDMRSKRVR SLLGRSLELN GAVEPSEGAP RAPPGPAGLS GGESLLVKQI 

       250        260        270        280        290        300 
EEQIKRNAAG KDGKERLGGS VLGQIPFLQN CEDEDSDEDD ELDSVQHKKQ RVKLPSKALV 

       310        320        330        340        350        360 
PEMEDEDEED DSEDAINEFD FLGSGEDGEG APDPRRCTVD GSPHELESRR VKLQGILADL 

       370        380        390        400        410        420 
RDVDGLPPKV TGPPPGTPQP RPHEDVFIMD TIGGGEVSLG DLADLTVTND NDLSCDLSDS 

       430        440        450        460        470        480 
KDAFKKTWNP KFTLRSHYDG IRSLAFHHSQ SALLTASEDG TLKLWNLQKA VTAKKNAALD 

       490        500        510        520        530        540 
VEPIHAFRAH RGPVLAVAMG SNSEYCYSGG ADACIHSWKI PDLSMDPYDG YDPSVLSHVL 

       550        560        570        580        590        600 
EGHGDAVWGL AFSPTSQRLA SCSADGTVRI WDPSSSSPAC LCTFPTASEH GVPTSVAFTS 

       610        620        630        640        650        660 
TEPAHIVASF RSGDTVLYDM EVGSALLTLE SRGSSGPTQI NQVVSHPNQP LTITAHDDRG 

       670        680        690        700        710        720 
IRFLDNRTGK PVHSMVAHLD AVTCLAVDPN GAFLMSGSHD CSLRLWSLDN KTCVQEITAH 

       730        740        750 
RKKHEEAIHA VACHPSKALI ASAGADALAK VFV 

« Hide

References

« Hide 'large scale' references
[1]"Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brain."
Castets F., Rakitina T., Gaillard S., Moqrich A., Mattei M.-G., Monneron A.
J. Biol. Chem. 275:19970-19977(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Muscle and Testis.
[3]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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-276, 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]"A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTTNBP2NL.
[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-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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].
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF212940 mRNA. Translation: AAF29527.1.
BC004910 mRNA. Translation: AAH04910.2.
BC034604 mRNA. Translation: AAH34604.1.
RefSeqNP_001034966.1. NM_001039877.1.
NP_037535.2. NM_013403.2.
UniGeneHs.631590.

3D structure databases

ProteinModelPortalQ9NRL3.
SMRQ9NRL3. Positions 409-752.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118941. 48 interactions.
IntActQ9NRL3. 54 interactions.
MINTMINT-1371553.
STRING9606.ENSP00000375777.

PTM databases

PhosphoSiteQ9NRL3.

Polymorphism databases

DMDM152031693.

Proteomic databases

PaxDbQ9NRL3.
PRIDEQ9NRL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263280; ENSP00000263280; ENSG00000090372.
GeneID29888.
KEGGhsa:29888.
UCSCuc002pfl.3. human.

Organism-specific databases

CTD29888.
GeneCardsGC19M047222.
H-InvDBHIX0096898.
HGNCHGNC:15721. STRN4.
HPAHPA043527.
HPA056706.
MIM614767. gene.
neXtProtNX_Q9NRL3.
PharmGKBPA134863218.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000236343.
HOVERGENHBG007117.
KOK17608.
OrthoDBEOG79KPDR.
PhylomeDBQ9NRL3.

Enzyme and pathway databases

SignaLinkQ9NRL3.

Gene expression databases

ArrayExpressQ9NRL3.
BgeeQ9NRL3.
CleanExHS_STRN4.
GenevestigatorQ9NRL3.

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. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTRN4. human.
GeneWikiSTRN4.
GenomeRNAi29888.
NextBio52431.
PMAP-CutDBQ9NRL3.
PROQ9NRL3.
SOURCESearch...

Entry information

Entry nameSTRN4_HUMAN
AccessionPrimary (citable) accession number: Q9NRL3
Secondary accession number(s): Q8NE53
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 123 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM