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Protein

Embryonal Fyn-associated substrate

Gene

Efs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES.

GO - Molecular functioni

  • protein domain specific binding Source: MGI
  • SH3 domain binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Embryonal Fyn-associated substrate
Alternative name(s):
SRC-interacting protein
Signal-integrating protein
Gene namesi
Name:Efs
Synonyms:Sin
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:105311. Efs.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi253 – 2531Y → F: Diminishes the ability to induce SRC-mediated activation of luciferase. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560Embryonal Fyn-associated substratePRO_0000086941Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei253 – 2531Phosphotyrosine; by SRC1 Publication

Post-translational modificationi

Phosphorylated on multiple tyrosine residues. Phosphorylated on tyrosines by FYN and SRC.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ64355.
PaxDbiQ64355.
PeptideAtlasiQ64355.
PRIDEiQ64355.

PTM databases

iPTMnetiQ64355.
PhosphoSiteiQ64355.

Expressioni

Tissue specificityi

Widely expressed. Higher levels found in placenta and embryo. Lower levels found in brain, brainstem, muscle and lung. No expression in liver and intestine.

Gene expression databases

BgeeiQ64355.
CleanExiMM_EFS.
GenevisibleiQ64355. MM.

Interactioni

GO - Molecular functioni

  • protein domain specific binding Source: MGI
  • SH3 domain binding Source: MGI

Protein-protein interaction databases

BioGridi199397. 4 interactions.
IntActiQ64355. 2 interactions.
MINTiMINT-100524.
STRINGi10090.ENSMUSP00000022813.

Structurei

3D structure databases

ProteinModelPortaliQ64355.
SMRiQ64355. Positions 9-74, 431-558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 6864SH3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni437 – 48751Divergent helix-loop-helix motifAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi304 – 3107SH3-bindingSequence analysis
Motifi334 – 3407SH3-bindingSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi67 – 355289Pro-richAdd
BLAST

Domaini

Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL SH2 domains.
The SH3-binding sites that bind to the SRC SH3 domain are required for interaction with CRK and are implicated in promotion of serum response element (SRE) activation. The SH3 domain interacts with PTK2/FAK1.

Sequence similaritiesi

Belongs to the CAS family.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiENOG410IEDN. Eukaryota.
ENOG410YE49. LUCA.
GeneTreeiENSGT00490000043324.
HOGENOMiHOG000054204.
HOVERGENiHBG003073.
InParanoidiQ64355.
OMAiPMAEEYD.
OrthoDBiEOG7QRQTD.
TreeFamiTF328782.

Family and domain databases

InterProiIPR021901. CAS_DUF3513.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12026. DUF3513. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64355-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIATSAQLA RALYDNTAES PQELSFRRGD VLRVLQREGA GGLDGWCLCS
60 70 80 90 100
LHGQQGIVPA NRVKLLPAGP APKPSLCPAS PTQPGSSCPT PERGCEEQEV
110 120 130 140 150
YVIPPPARPC SASGLPARSC SPSSDSIYKV PRGNGMQLTA SRDVAEVYDV
160 170 180 190 200
PPNILRAPSS CPYDSPASFS CPVAPVVPQP PREDEAPYDV PLALKPPAEL
210 220 230 240 250
ERDPEWEGGR EPGPPLYAAP SNLKRASALL NLYEAPEELL ANGESRDADE
260 270 280 290 300
GIYDVPLLGP EPPSPEPPVA SSSTDLDTVA QLPTRSSPPQ HRPRLPSTES
310 320 330 340 350
LSRRPLPALP VSEAPAPSPA PSPAPGRKGS IQDRPLPPPP PCLPGYGGLK
360 370 380 390 400
PEGDPECREV ANDPAGPHNE YEGIPMAEEY DYVHLKGVDT AQGSRPLDKA
410 420 430 440 450
FPVDPELLER GLAERKEALS PEEPLVLSTG DLQLLHFYAG QCQSHYSALQ
460 470 480 490 500
AAVAALVAST QANQPPCLFV PHGKRVVVAA HRLVFVGDTL GRLAASAALR
510 520 530 540 550
AQVGAAGTML AQTLRATVLA VKGAALGYPS DTAVQEMARC VAELAGQALR
560
FTTLLDGLLP
Length:560
Mass (Da):58,973
Last modified:July 27, 2011 - v2
Checksum:iDC9D6C9DF2B9DF1F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331G → V in AAB02246 (PubMed:8647432).Curated
Sequence conflicti133 – 1331G → V in AAC52340 (PubMed:8570184).Curated
Sequence conflicti133 – 1331G → V in AAH05438 (PubMed:15489334).Curated
Sequence conflicti556 – 5561D → A in AAB02246 (PubMed:8647432).Curated
Sequence conflicti556 – 5561D → A in AAC52340 (PubMed:8570184).Curated
Sequence conflicti556 – 5561D → A in AAH05438 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57686 mRNA. Translation: AAB02246.1.
U28728 mRNA. Translation: AAC52340.1.
AK030321 mRNA. Translation: BAC26900.1.
AK163191 mRNA. Translation: BAE37228.1.
BC005438 mRNA. Translation: AAH05438.1.
CCDSiCCDS36925.1.
RefSeqiNP_034242.2. NM_010112.4.
UniGeneiMm.236438.

Genome annotation databases

EnsembliENSMUST00000022813; ENSMUSP00000022813; ENSMUSG00000022203.
GeneIDi13644.
KEGGimmu:13644.
UCSCiuc007txm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57686 mRNA. Translation: AAB02246.1.
U28728 mRNA. Translation: AAC52340.1.
AK030321 mRNA. Translation: BAC26900.1.
AK163191 mRNA. Translation: BAE37228.1.
BC005438 mRNA. Translation: AAH05438.1.
CCDSiCCDS36925.1.
RefSeqiNP_034242.2. NM_010112.4.
UniGeneiMm.236438.

3D structure databases

ProteinModelPortaliQ64355.
SMRiQ64355. Positions 9-74, 431-558.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199397. 4 interactions.
IntActiQ64355. 2 interactions.
MINTiMINT-100524.
STRINGi10090.ENSMUSP00000022813.

PTM databases

iPTMnetiQ64355.
PhosphoSiteiQ64355.

Proteomic databases

MaxQBiQ64355.
PaxDbiQ64355.
PeptideAtlasiQ64355.
PRIDEiQ64355.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022813; ENSMUSP00000022813; ENSMUSG00000022203.
GeneIDi13644.
KEGGimmu:13644.
UCSCiuc007txm.2. mouse.

Organism-specific databases

CTDi10278.
MGIiMGI:105311. Efs.

Phylogenomic databases

eggNOGiENOG410IEDN. Eukaryota.
ENOG410YE49. LUCA.
GeneTreeiENSGT00490000043324.
HOGENOMiHOG000054204.
HOVERGENiHBG003073.
InParanoidiQ64355.
OMAiPMAEEYD.
OrthoDBiEOG7QRQTD.
TreeFamiTF328782.

Miscellaneous databases

ChiTaRSiEfs. mouse.
PROiQ64355.
SOURCEiSearch...

Gene expression databases

BgeeiQ64355.
CleanExiMM_EFS.
GenevisibleiQ64355. MM.

Family and domain databases

InterProiIPR021901. CAS_DUF3513.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF12026. DUF3513. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel p130Cas-related protein, Sin."
    Alexandropoulos K., Baltimore D.
    Genes Dev. 10:1341-1355(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT TYR-253, MUTAGENESIS OF TYR-253.
    Tissue: Embryo.
  2. "Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn."
    Ishino M., Ohba T., Sasaki H., Sasaki T.
    Oncogene 11:2331-2338(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
    Tissue: Embryo.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Ovary and Uterus.
  4. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung.

Entry informationi

Entry nameiEFS_MOUSE
AccessioniPrimary (citable) accession number: Q64355
Secondary accession number(s): Q8BSX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 119 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

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.