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Protein

Espin

Gene

Espn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional actin-bundling protein. Plays a major role in regulating the organization, dimensions, dynamics and signaling capacities of the actin filament-rich, microvillus-type specializations that mediate sensory transduction in variouS mechanosensory and chemosensory cells.2 Publications

GO - Molecular functioni

GO - Biological processi

  • actin filament bundle assembly Source: MGI
  • actin filament network formation Source: UniProtKB
  • locomotory behavior Source: MGI
  • negative regulation of cytoskeleton organization Source: UniProtKB
  • parallel actin filament bundle assembly Source: MGI
  • positive regulation of filopodium assembly Source: MGI
  • sensory perception of sound Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Hearing

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Espin
Alternative name(s):
Ectoplasmic specialization protein
Gene namesi
Name:Espn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1861630. Espn.

Subcellular locationi

Isoform 8 :
  • Cytoplasmcytoskeleton
  • Cell junction

  • Note: Isoform 8 localizes to parallel actin bundles of ectoplasmic specializations between neighboring Sertoli cells and at sites where Sertoli cells contact the heads of elongate spermatids.

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • brush border Source: UniProtKB
  • cell junction Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • dendritic spine Source: UniProtKB-SubCell
  • filamentous actin Source: UniProtKB
  • microvillus Source: MGI
  • stereocilium bundle Source: MGI
  • stereocilium tip Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 871871EspinPRO_0000334667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei338 – 3381PhosphoserineBy similarity
Modified residuei342 – 3421PhosphoserineCombined sources
Modified residuei517 – 5171PhosphoserineBy similarity
Modified residuei524 – 5241PhosphoserineBy similarity
Modified residuei665 – 6651PhosphoserineCombined sources
Modified residuei704 – 7041PhosphoserineCombined sources
Modified residuei708 – 7081PhosphoserineCombined sources
Modified residuei714 – 7141PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9ET47.
MaxQBiQ9ET47.
PaxDbiQ9ET47.
PRIDEiQ9ET47.

PTM databases

iPTMnetiQ9ET47.
PhosphoSiteiQ9ET47.

Expressioni

Tissue specificityi

Expressed at high concentration in the microvillar parallel actin bundle (PAB) of hair cells stereocilia in the cochlea and vestibular system. Detected also at high levels of a number of other sensory cell types, including taste receptor cells, solitary chemoreceptor cells, vomeronasal sensory neurons and Merkel cells. Isoforms 2, 3, 4 and 5 are expressed in Purkinje cells dentritic spines.3 Publications

Gene expression databases

BgeeiQ9ET47.
ExpressionAtlasiQ9ET47. baseline and differential.
GenevisibleiQ9ET47. MM.

Interactioni

Subunit structurei

Monomer. Binds F-actin in a Ca2+-resistant fashion. Interacts (via N-terminal) with BAIAP2 (via SH3-domain). Interacts with PFN2.3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207859. 8 interactions.
IntActiQ9ET47. 9 interactions.
MINTiMINT-258237.
STRINGi10090.ENSMUSP00000030785.

Structurei

Secondary structure

871
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 1212Combined sources
Helixi15 – 239Combined sources
Helixi39 – 446Combined sources
Turni45 – 473Combined sources
Helixi49 – 579Combined sources
Helixi73 – 808Combined sources
Helixi83 – 908Combined sources
Turni91 – 933Combined sources
Helixi107 – 1137Combined sources
Helixi117 – 1259Combined sources
Helixi141 – 1488Combined sources
Helixi151 – 16010Combined sources
Helixi162 – 1643Combined sources
Helixi175 – 1817Combined sources
Helixi185 – 19511Combined sources
Helixi209 – 2157Combined sources
Helixi219 – 22810Combined sources
Helixi243 – 2497Combined sources
Helixi253 – 2619Combined sources
Helixi275 – 2817Combined sources
Helixi285 – 2939Combined sources
Helixi308 – 3147Combined sources
Helixi318 – 32912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ET0X-ray2.30A/C1-352[»]
5ET1X-ray1.65A/B1-352[»]
ProteinModelPortaliQ9ET47.
SMRiQ9ET47. Positions 4-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 3131ANK 1Add
BLAST
Repeati35 – 6632ANK 2Add
BLAST
Repeati69 – 9931ANK 3Add
BLAST
Repeati103 – 13230ANK 4Add
BLAST
Repeati137 – 16731ANK 5Add
BLAST
Repeati171 – 20131ANK 6Add
BLAST
Repeati205 – 23531ANK 7Add
BLAST
Repeati239 – 26830ANK 8Add
BLAST
Repeati271 – 30030ANK 9Add
BLAST
Domaini669 – 68618WH2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili772 – 84877Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi428 – 46538Pro-richAdd
BLAST
Compositional biasi607 – 62923Pro-richAdd
BLAST
Compositional biasi642 – 6454Poly-Ser

Domaini

The WH2-domain binds actin monomer and mediates actin bundle assembly.

Sequence similaritiesi

Contains 9 ANK repeats.PROSITE-ProRule annotation
Contains 1 WH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00600000084407.
HOVERGENiHBG100662.
InParanoidiQ9ET47.
OrthoDBiEOG7353WF.
PhylomeDBiQ9ET47.
TreeFamiTF326392.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR030233. Espn.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR24153:SF14. PTHR24153:SF14. 2 hits.
PfamiPF12796. Ank_2. 2 hits.
PF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 9 hits.
SM00246. WH2. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51082. WH2. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ET47-1) [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
MALEQALQAA RRGDLDVLRS LHAAGLLGPS LRDSLDALPV HHAARSGKLH
60 70 80 90 100
CLRYLVEEVA LPAVSRARNG ATPAHDAAAT GYLSCLQWLL TQGGCRVQEK
110 120 130 140 150
DNSGATVLHL AARFGHPDVV KWLLYQGGAN SAITTDTGAL PIHYAAAKGD
160 170 180 190 200
LPSLKLLVGH YPEGVNAQTN NGATPLYLAC QEGHLEVTKY LVQECSADPH
210 220 230 240 250
LRAQDGMTPL HAAAQMGHNP VLVWLVSFAD VSFSEQDHDG ATAMHFAASR
260 270 280 290 300
GHTKVLSWLL LHGAEISQDL WGGTPLHDAA ENGELECCQI LAVNGAGLDV
310 320 330 340 350
RDHDGYTAAD LAEFNGHTHC SRYLRTVQTL SLEHRVLSRD QSMDLEAKQL
360 370 380 390 400
DSGMSSPNTT MSVQPMTFDL GSPTSTFSNY DSCSSSHSSS KGQRSNRGIP
410 420 430 440 450
GARAADLQSY MDMLNPEKSL PRGKLGKPSP PPPPPPPPPS FPPPPPPTGT
460 470 480 490 500
QPPPPPPGYP APNPPVGLHL NNIYMQTKNK LRHVEVDSLK EPKVELNDQF
510 520 530 540 550
AQPSSGDGHS GLHRQDSGLL RQDSELLHRQ ELLRHSTGLR RQDSDRKQRS
560 570 580 590 600
FSKQPSTGDY YRQLGRSPGE PLAARPGMAH SEEAALLPGN HVHNGCSADS
610 620 630 640 650
KASRELPPPP PPPPLPEALS SPPPAPPLPI EGAGAACGQR RSSSSTGKVR
660 670 680 690 700
VLRHRKSTKS FNMMSPTGDN SELLAEIKAG KSLKPTPQSK GLTTVFSGSG
710 720 730 740 750
QPASQPESPQ PLVSPAPSRT RSPTPPASGS QPLLNGSVVP APPATPAPGV
760 770 780 790 800
HLDVEALIPT LDEQGRPIPE WKRQVMVRKL QQKMQEEEEQ RRKEEEEEAR
810 820 830 840 850
LASLPAWRRD ILRKKLEEER EQKRKEEERQ KLEEIQRAKE QSEKLRTLGY
860 870
DEAKLAPWQR QVILKKGEIP K
Length:871
Mass (Da):94,497
Last modified:May 20, 2008 - v2
Checksum:iC7707D5C73678DA1
GO
Isoform 2 (identifier: Q9ET47-2) [UniParc]FASTAAdd to basket

Also known as: Purkinje cell espin isoform 1

The sequence of this isoform differs from the canonical sequence as follows:
     1-327: Missing.
     328-330: QTL → MGN
     492-502: Missing.
     648-656: Missing.

Show »
Length:524
Mass (Da):57,110
Checksum:i1E8E73310C9FF73A
GO
Isoform 3 (identifier: Q9ET47-3) [UniParc]FASTAAdd to basket

Also known as: Purkinje cell espin isoform 1+

The sequence of this isoform differs from the canonical sequence as follows:
     1-327: Missing.
     328-330: QTL → MGN
     492-502: Missing.

Show »
Length:533
Mass (Da):58,284
Checksum:iB6C766CA2E809B12
GO
Isoform 4 (identifier: Q9ET47-4) [UniParc]FASTAAdd to basket

Also known as: Purkinje cell espin isoform 2+

The sequence of this isoform differs from the canonical sequence as follows:
     1-327: Missing.
     328-330: QTL → MGN
     492-583: Missing.

Show »
Length:452
Mass (Da):49,195
Checksum:i6BF7A17610ADB308
GO
Isoform 5 (identifier: Q9ET47-5) [UniParc]FASTAAdd to basket

Also known as: Purkinje cell espin isoform 2

The sequence of this isoform differs from the canonical sequence as follows:
     1-327: Missing.
     328-330: QTL → MGN
     492-583: Missing.
     648-656: Missing.

Show »
Length:443
Mass (Da):48,021
Checksum:iC1E65EA9DF270594
GO
Isoform 6 (identifier: Q9ET47-6) [UniParc]FASTAAdd to basket

Also known as: 3B

The sequence of this isoform differs from the canonical sequence as follows:
     1-547: Missing.
     548-583: QRSFSKQPSTGDYYRQLGRSPGEPLAARPGMAHSEE → MAHSEEVRVHQPALAGCSGPSPVPRPSLSGPSAPPQ
     648-656: Missing.

Show »
Length:315
Mass (Da):34,039
Checksum:i881DAD36A6CC0FCF
GO
Isoform 7 (identifier: Q9ET47-7) [UniParc]FASTAAdd to basket

Also known as: 3A

The sequence of this isoform differs from the canonical sequence as follows:
     1-577: Missing.
     648-656: Missing.

Show »
Length:285
Mass (Da):31,109
Checksum:i8F41844768B6884D
GO
Isoform 8 (identifier: Q9ET47-8) [UniParc]FASTAAdd to basket

Also known as: small

The sequence of this isoform differs from the canonical sequence as follows:
     1-643: Missing.
     644-656: SSTGKVRVLRHRK → MNSQGPLGGGRIP
     705-705: Q → QVGTGRVPRPGSQCLPSAQPYCFSRQ

Show »
Length:253
Mass (Da):28,116
Checksum:iC7AE5E342801385C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti564 – 5641L → M in AAO50326 (PubMed:12598619).Curated
Sequence conflicti564 – 5641L → M in AAO50327 (PubMed:12598619).Curated
Sequence conflicti564 – 5641L → M in AAF98134 (PubMed:10975527).Curated
Sequence conflicti720 – 7201T → A in AAF18322 (PubMed:10588661).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 643643Missing in isoform 8. CuratedVSP_033730Add
BLAST
Alternative sequencei1 – 577577Missing in isoform 7. 1 PublicationVSP_033731Add
BLAST
Alternative sequencei1 – 547547Missing in isoform 6. 1 PublicationVSP_033732Add
BLAST
Alternative sequencei1 – 327327Missing in isoform 2, isoform 4, isoform 3 and isoform 5. 1 PublicationVSP_033733Add
BLAST
Alternative sequencei328 – 3303QTL → MGN in isoform 2, isoform 4, isoform 3 and isoform 5. 1 PublicationVSP_033734
Alternative sequencei492 – 58392Missing in isoform 4 and isoform 5. 1 PublicationVSP_033735Add
BLAST
Alternative sequencei492 – 50211Missing in isoform 2 and isoform 3. 1 PublicationVSP_033736Add
BLAST
Alternative sequencei548 – 58336QRSFS…AHSEE → MAHSEEVRVHQPALAGCSGP SPVPRPSLSGPSAPPQ in isoform 6. 1 PublicationVSP_033737Add
BLAST
Alternative sequencei644 – 65613SSTGK…LRHRK → MNSQGPLGGGRIP in isoform 8. CuratedVSP_033738Add
BLAST
Alternative sequencei648 – 6569Missing in isoform 2, isoform 5, isoform 6 and isoform 7. 2 PublicationsVSP_033739
Alternative sequencei705 – 7051Q → QVGTGRVPRPGSQCLPSAQP YCFSRQ in isoform 8. CuratedVSP_033740

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239886 mRNA. Translation: AAF98134.1.
AF540942 mRNA. Translation: AAO50326.1.
AF540943 mRNA. Translation: AAO50327.1.
AF540944 mRNA. Translation: AAO50328.1.
AF540945 mRNA. Translation: AAO50329.1.
AY587570 mRNA. Translation: AAT46472.1.
AY587571 mRNA. Translation: AAT46473.1.
AF134858 Genomic DNA. Translation: AAF18322.1.
AL772240 Genomic DNA. Translation: CAM19680.1.
AL772240 Genomic DNA. Translation: CAM19684.1.
AL772240 Genomic DNA. Translation: CAM19685.1.
AL772240 Genomic DNA. Translation: CAM19686.1.
AL772240 Genomic DNA. Translation: CAM19687.1.
AL772240 Genomic DNA. Translation: CAM19691.1.
CCDSiCCDS18989.1. [Q9ET47-1]
CCDS18990.1. [Q9ET47-3]
CCDS18991.1. [Q9ET47-4]
CCDS18992.1. [Q9ET47-5]
CCDS18993.1. [Q9ET47-2]
CCDS18994.1. [Q9ET47-8]
RefSeqiNP_997570.1. NM_207687.2. [Q9ET47-1]
NP_997571.1. NM_207688.2. [Q9ET47-3]
NP_997572.1. NM_207689.2. [Q9ET47-4]
NP_997573.1. NM_207690.2. [Q9ET47-5]
NP_997574.2. NM_207691.2. [Q9ET47-2]
UniGeneiMm.264215.

Genome annotation databases

EnsembliENSMUST00000030785; ENSMUSP00000030785; ENSMUSG00000028943. [Q9ET47-1]
ENSMUST00000070018; ENSMUSP00000065545; ENSMUSG00000028943. [Q9ET47-2]
ENSMUST00000080042; ENSMUSP00000078951; ENSMUSG00000028943. [Q9ET47-4]
ENSMUST00000084114; ENSMUSP00000081131; ENSMUSG00000028943. [Q9ET47-3]
ENSMUST00000105653; ENSMUSP00000101278; ENSMUSG00000028943. [Q9ET47-7]
ENSMUST00000105657; ENSMUSP00000101282; ENSMUSG00000028943. [Q9ET47-5]
GeneIDi56226.
KEGGimmu:56226.
UCSCiuc008vzn.1. mouse. [Q9ET47-6]
uc008vzo.1. mouse. [Q9ET47-7]
uc008vzp.1. mouse. [Q9ET47-4]
uc008vzq.1. mouse. [Q9ET47-3]
uc008vzr.1. mouse. [Q9ET47-5]
uc008vzs.1. mouse. [Q9ET47-2]
uc008vzt.1. mouse. [Q9ET47-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF239886 mRNA. Translation: AAF98134.1.
AF540942 mRNA. Translation: AAO50326.1.
AF540943 mRNA. Translation: AAO50327.1.
AF540944 mRNA. Translation: AAO50328.1.
AF540945 mRNA. Translation: AAO50329.1.
AY587570 mRNA. Translation: AAT46472.1.
AY587571 mRNA. Translation: AAT46473.1.
AF134858 Genomic DNA. Translation: AAF18322.1.
AL772240 Genomic DNA. Translation: CAM19680.1.
AL772240 Genomic DNA. Translation: CAM19684.1.
AL772240 Genomic DNA. Translation: CAM19685.1.
AL772240 Genomic DNA. Translation: CAM19686.1.
AL772240 Genomic DNA. Translation: CAM19687.1.
AL772240 Genomic DNA. Translation: CAM19691.1.
CCDSiCCDS18989.1. [Q9ET47-1]
CCDS18990.1. [Q9ET47-3]
CCDS18991.1. [Q9ET47-4]
CCDS18992.1. [Q9ET47-5]
CCDS18993.1. [Q9ET47-2]
CCDS18994.1. [Q9ET47-8]
RefSeqiNP_997570.1. NM_207687.2. [Q9ET47-1]
NP_997571.1. NM_207688.2. [Q9ET47-3]
NP_997572.1. NM_207689.2. [Q9ET47-4]
NP_997573.1. NM_207690.2. [Q9ET47-5]
NP_997574.2. NM_207691.2. [Q9ET47-2]
UniGeneiMm.264215.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ET0X-ray2.30A/C1-352[»]
5ET1X-ray1.65A/B1-352[»]
ProteinModelPortaliQ9ET47.
SMRiQ9ET47. Positions 4-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207859. 8 interactions.
IntActiQ9ET47. 9 interactions.
MINTiMINT-258237.
STRINGi10090.ENSMUSP00000030785.

PTM databases

iPTMnetiQ9ET47.
PhosphoSiteiQ9ET47.

Proteomic databases

EPDiQ9ET47.
MaxQBiQ9ET47.
PaxDbiQ9ET47.
PRIDEiQ9ET47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030785; ENSMUSP00000030785; ENSMUSG00000028943. [Q9ET47-1]
ENSMUST00000070018; ENSMUSP00000065545; ENSMUSG00000028943. [Q9ET47-2]
ENSMUST00000080042; ENSMUSP00000078951; ENSMUSG00000028943. [Q9ET47-4]
ENSMUST00000084114; ENSMUSP00000081131; ENSMUSG00000028943. [Q9ET47-3]
ENSMUST00000105653; ENSMUSP00000101278; ENSMUSG00000028943. [Q9ET47-7]
ENSMUST00000105657; ENSMUSP00000101282; ENSMUSG00000028943. [Q9ET47-5]
GeneIDi56226.
KEGGimmu:56226.
UCSCiuc008vzn.1. mouse. [Q9ET47-6]
uc008vzo.1. mouse. [Q9ET47-7]
uc008vzp.1. mouse. [Q9ET47-4]
uc008vzq.1. mouse. [Q9ET47-3]
uc008vzr.1. mouse. [Q9ET47-5]
uc008vzs.1. mouse. [Q9ET47-2]
uc008vzt.1. mouse. [Q9ET47-1]

Organism-specific databases

CTDi83715.
MGIiMGI:1861630. Espn.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00600000084407.
HOVERGENiHBG100662.
InParanoidiQ9ET47.
OrthoDBiEOG7353WF.
PhylomeDBiQ9ET47.
TreeFamiTF326392.

Miscellaneous databases

PROiQ9ET47.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ET47.
ExpressionAtlasiQ9ET47. baseline and differential.
GenevisibleiQ9ET47. MM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR030233. Espn.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR24153:SF14. PTHR24153:SF14. 2 hits.
PfamiPF12796. Ank_2. 2 hits.
PF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00248. ANK. 9 hits.
SM00246. WH2. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51082. WH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The deaf jerker mouse has a mutation in the gene encoding the espin actin-bundling proteins of hair cell stereocilia and lacks espins."
    Zheng L., Sekerkova G., Vranich K., Tilney L.G., Mugnaini E., Bartles J.R.
    Cell 102:377-385(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Novel espin actin-bundling proteins are localized to Purkinje cell dendritic spines and bind the Src homology 3 adapter protein insulin receptor substrate p53."
    Sekerkova G., Loomis P.A., Changyaleket B., Zheng L., Eytan R., Chen B., Mugnaini E., Bartles J.R.
    J. Neurosci. 23:1310-1319(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH BAIAP2.
    Strain: CBA/CaJ.
    Tissue: Cerebellum.
  3. "Espins are multifunctional actin cytoskeletal regulatory proteins in the microvilli of chemosensory and mechanosensory cells."
    Sekerkova G., Zheng L., Loomis P.A., Changyaleket B., Whitlon D.S., Mugnaini E., Bartles J.R.
    J. Neurosci. 24:5445-5456(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), FUNCTION, INTERACTION WITH PFN2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: CD-1.
  4. "Espin contains an additional actin-binding site in its N terminus and is a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization junctional plaque."
    Chen B., Li A., Wang D., Wang M., Zheng L., Bartles J.R.
    Mol. Biol. Cell 10:4327-4339(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 8), SUBUNIT.
    Strain: 129/SvJ.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "Espin cross-links cause the elongation of microvillus-type parallel actin bundles in vivo."
    Loomis P.A., Zheng L., Sekerkova G., Changyaleket B., Mugnaini E., Bartles J.R.
    J. Cell Biol. 163:1045-1055(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-665; SER-704 AND SER-708, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiESPN_MOUSE
AccessioniPrimary (citable) accession number: Q9ET47
Secondary accession number(s): A2AK06
, A2AK09, A2AK13, B1AWP3, B1AWP6, B1AWQ2, Q6GYS0, Q6GYS1, Q80ZC0, Q80ZC1, Q80ZC2, Q80ZC3, Q9QY27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 8, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Jerker mice has a frameshift mutation that affect the espin C-terminus. This mutation cause deafness, vestibular dysfunction and hair cell degeneration.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.