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Protein

Striatin

Gene

STRN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. armadillo repeat domain binding Source: UniProtKB
  2. calmodulin binding Source: UniProtKB
  3. estrogen receptor binding Source: UniProtKB
  4. protein complex binding Source: UniProtKB
  5. protein phosphatase 2A binding Source: UniProtKB

GO - Biological processi

  1. dendrite development Source: UniProtKB
  2. locomotory behavior Source: UniProtKB
  3. negative regulation of cell proliferation Source: UniProtKB
  4. tight junction assembly Source: UniProtKB
  5. Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

SignaLinkiO43815.

Names & Taxonomyi

Protein namesi
Recommended name:
Striatin
Gene namesi
Name:STRN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11424. STRN.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Membrane By similarity; Peripheral membrane protein By similarity
  3. Cell projectiondendritic spine By similarity

  4. Note: CTTNBP2-binding may regulate dendritic spine distribution.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. dendritic spine Source: UniProtKB
  3. membrane Source: UniProtKB
  4. neuronal cell body Source: UniProtKB
  5. postsynaptic density Source: UniProtKB
  6. postsynaptic membrane Source: UniProtKB
  7. tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36224.

Polymorphism and mutation databases

BioMutaiSTRN.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 780780StriatinPRO_0000051232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei245 – 2451Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO43815.
PaxDbiO43815.
PRIDEiO43815.

PTM databases

PhosphoSiteiO43815.

Miscellaneous databases

PMAP-CutDBO43815.

Expressioni

Tissue specificityi

Preferentially expressed in brain.1 Publication

Gene expression databases

BgeeiO43815.
CleanExiHS_STRN.
GenevestigatoriO43815.

Organism-specific databases

HPAiHPA017286.

Interactioni

Subunit structurei

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).By similarityCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
CTTNBP2NLQ9P2B45EBI-1046642,EBI-1774273
MOB4Q9Y3A34EBI-1046642,EBI-713935
PDCD10Q9BUL83EBI-1046642,EBI-740195
PPP2CAP677753EBI-1046642,EBI-712311
PPP2R1AP301534EBI-1046642,EBI-302388
RINT1Q6NUQ13EBI-1046642,EBI-726876
STK24Q9Y6E03EBI-1046642,EBI-740175
STK25O005063EBI-1046642,EBI-618295
STRN3Q130337EBI-1046642,EBI-1053857
TFIP11Q9UBB93EBI-1046642,EBI-1105213
TNKS2Q9H2K22EBI-1046642,EBI-4398527
TRAF3IP3Q9Y2282EBI-1046642,EBI-765817

Protein-protein interaction databases

BioGridi112674. 57 interactions.
IntActiO43815. 39 interactions.
MINTiMINT-2796380.
STRINGi9606.ENSP00000263918.

Structurei

3D structure databases

ProteinModelPortaliO43815.
SMRiO43815. Positions 70-114, 401-779.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati461 – 50040WD 1Add
BLAST
Repeati514 – 55340WD 2Add
BLAST
Repeati567 – 60640WD 3Add
BLAST
Repeati662 – 70140WD 4Add
BLAST
Repeati704 – 74340WD 5Add
BLAST
Repeati750 – 77930WD 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 639Caveolin-bindingSequence Analysis
Regioni149 – 16618Calmodulin-bindingSequence AnalysisAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili53 – 12068Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat striatin family.Curated
Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00520000055597.
HOGENOMiHOG000236343.
HOVERGENiHBG007117.
InParanoidiO43815.
KOiK17608.
OMAiTDWEKDE.
OrthoDBiEOG79KPDR.
PhylomeDBiO43815.
TreeFamiTF313387.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. 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]
PfamiPF08232. Striatin. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43815-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MDEQAGPGVF FSNNHPGAGG AKGLGPLAEA AAAGDGAAAA GAARAQYSLP
60 70 80 90 100
GILHFLQHEW ARFEVERAQW EVERAELQAQ IAFLQGERKG QENLKKDLVR
110 120 130 140 150
RIKMLEYALK QERAKYHKLK YGTELNQGDM KPPSYDSDEG NETEVQPQQN
160 170 180 190 200
SQLMWKQGRQ LLRQYLQEVG YTDTILDVKS KRVRALLGFS SDVTDREDDK
210 220 230 240 250
NQDSVVNGTE AEVKETAMIA KSELTDSASV LDNFKFLESA AADFSDEDED
260 270 280 290 300
DDVDGREKSV IDTSTIVRKK ALPDSGEDRD TKEALKEFDF LVTSEEGDNE
310 320 330 340 350
SRSAGDGTDW EKEDQCLMPE AWNVDQGVIT KLKEQYKKER KGKKGVKRPN
360 370 380 390 400
RSKLQDMLAN LRDVDELPSL QPSVGSPSRP SSSRLPEHEI NRADEVEALT
410 420 430 440 450
FPPSSGKSFI MGADEALESE LGLGELAGLT VANEADSLTY DIANNKDALR
460 470 480 490 500
KTWNPKFTLR SHFDGIRALA FHPIEPVLIT ASEDHTLKMW NLQKTAPAKK
510 520 530 540 550
STSLDVEPIY TFRAHKGPVL CVVMSSNGEQ CYSGGTDGLI QGWNTTNPNI
560 570 580 590 600
DPYDSYDPSV LRGPLLGHTD AVWGLAYSAA HQRLLSCSAD GTLRLWNTTE
610 620 630 640 650
VAPALSVFND TKELGIPASV DLVSSDPSHM VASFSKGYTS IFNMETQQRI
660 670 680 690 700
LTLESNVDTT ANSSCQINRV ISHPTLPISI TAHEDRHIKF YDNNTGKLIH
710 720 730 740 750
SMVAHLEAVT SLAVDPNGLY LMSGSHDCSI RLWNLESKTC IQEFTAHRKK
760 770 780
FEESIHDVAF HPSKCYIASA GADALAKVFV
Length:780
Mass (Da):86,132
Last modified:March 6, 2007 - v4
Checksum:iDDB18A11102BEA35
GO
Isoform 2 (identifier: O43815-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     29-40: Missing.
     311-348: EKEDQCLMPEAWNVDQGVITKLKEQYKKERKGKKGVKR → G

Note: No experimental confirmation available.

Show »
Length:731
Mass (Da):80,761
Checksum:i67B5DD94E3499AB7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911S → I in CAA11560 (PubMed:9693043).Curated
Sequence conflicti423 – 4231L → P in CAA11560 (PubMed:9693043).Curated
Sequence conflicti611 – 6111T → I in CAA11560 (PubMed:9693043).Curated
Sequence conflicti677 – 6771P → S in CAA11560 (PubMed:9693043).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei29 – 4012Missing in isoform 2. 1 PublicationVSP_023495Add
BLAST
Alternative sequencei311 – 34838EKEDQ…KGVKR → G in isoform 2. 1 PublicationVSP_023496Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223814 mRNA. Translation: CAA11560.1.
AC007404 Genomic DNA. Translation: AAY24273.1.
AC007382 Genomic DNA. Translation: AAF66162.1.
BC106879 mRNA. Translation: AAI06880.1.
CCDSiCCDS1784.1. [O43815-1]
RefSeqiNP_003153.2. NM_003162.3. [O43815-1]
UniGeneiHs.127486.

Genome annotation databases

EnsembliENST00000263918; ENSP00000263918; ENSG00000115808. [O43815-1]
ENST00000379213; ENSP00000368513; ENSG00000115808. [O43815-2]
GeneIDi6801.
KEGGihsa:6801.
UCSCiuc002rpn.3. human. [O43815-1]
uc010ezx.3. human. [O43815-2]

Polymorphism and mutation databases

BioMutaiSTRN.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223814 mRNA. Translation: CAA11560.1.
AC007404 Genomic DNA. Translation: AAY24273.1.
AC007382 Genomic DNA. Translation: AAF66162.1.
BC106879 mRNA. Translation: AAI06880.1.
CCDSiCCDS1784.1. [O43815-1]
RefSeqiNP_003153.2. NM_003162.3. [O43815-1]
UniGeneiHs.127486.

3D structure databases

ProteinModelPortaliO43815.
SMRiO43815. Positions 70-114, 401-779.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112674. 57 interactions.
IntActiO43815. 39 interactions.
MINTiMINT-2796380.
STRINGi9606.ENSP00000263918.

PTM databases

PhosphoSiteiO43815.

Polymorphism and mutation databases

BioMutaiSTRN.

Proteomic databases

MaxQBiO43815.
PaxDbiO43815.
PRIDEiO43815.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263918; ENSP00000263918; ENSG00000115808. [O43815-1]
ENST00000379213; ENSP00000368513; ENSG00000115808. [O43815-2]
GeneIDi6801.
KEGGihsa:6801.
UCSCiuc002rpn.3. human. [O43815-1]
uc010ezx.3. human. [O43815-2]

Organism-specific databases

CTDi6801.
GeneCardsiGC02M036987.
HGNCiHGNC:11424. STRN.
HPAiHPA017286.
MIMi614765. gene.
neXtProtiNX_O43815.
PharmGKBiPA36224.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00520000055597.
HOGENOMiHOG000236343.
HOVERGENiHBG007117.
InParanoidiO43815.
KOiK17608.
OMAiTDWEKDE.
OrthoDBiEOG79KPDR.
PhylomeDBiO43815.
TreeFamiTF313387.

Enzyme and pathway databases

SignaLinkiO43815.

Miscellaneous databases

ChiTaRSiSTRN. human.
GeneWikiiSTRN.
GenomeRNAii6801.
NextBioi26559.
PMAP-CutDBO43815.
PROiO43815.
SOURCEiSearch...

Gene expression databases

BgeeiO43815.
CleanExiHS_STRN.
GenevestigatoriO43815.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. 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]
PfamiPF08232. Striatin. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSTRN_HUMAN
AccessioniPrimary (citable) accession number: O43815
Secondary accession number(s): Q3KP65, Q53TQ8, Q9NP38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 6, 2007
Last modified: April 29, 2015
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.