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Q9Z2H5 (E41L1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Band 4.1-like protein 1
Alternative name(s):
Neuronal protein 4.1
Short name=4.1N
Gene names
Name:Epb41l1
Synonyms:Epb4, Epb4.1l1, Kiaa0338
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length879 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases.

Subunit structure

Interacts with AGAP2 By similarity.

Subcellular location

Cytoplasm › cytoskeleton.

Tissue specificity

Highest expression in brain, also present in kidney, olfactory epithelium, retina, sensory ganglia, gastrointestinal tract (only enteric neurons) and lung.

Sequence similarities

Contains 1 FERM domain.

Sequence caution

The sequence BAC65533.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcortical actin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic to membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Z2H5-1)

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: Q9Z2H5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     484-495: Missing.
Isoform 3 (identifier: Q9Z2H5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     484-495: Missing.
     556-691: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 879879Band 4.1-like protein 1
PRO_0000219396

Regions

Domain97 – 378282FERM
Region381 – 482102Hydrophilic
Region483 – 54159Spectrin--actin-binding
Region743 – 879137C-terminal (CTD)

Amino acid modifications

Modified residue751Phosphoserine By similarity
Modified residue791Phosphothreonine By similarity
Modified residue3431Phosphotyrosine Ref.9
Modified residue3781Phosphoserine Ref.10
Modified residue4301Phosphoserine Ref.11
Modified residue4661Phosphoserine Ref.6
Modified residue4751Phosphothreonine Ref.6
Modified residue5101Phosphoserine Ref.11
Modified residue5401Phosphoserine By similarity
Modified residue5411Phosphoserine By similarity
Modified residue5441Phosphoserine By similarity
Modified residue5461Phosphoserine Ref.6 Ref.7
Modified residue5501Phosphothreonine Ref.6 Ref.7
Modified residue5641Phosphoserine By similarity
Modified residue5781Phosphoserine By similarity
Modified residue6391Phosphoserine Ref.11
Modified residue6481Phosphoserine Ref.6 Ref.7
Modified residue6501Phosphoserine Ref.6 Ref.10
Modified residue6771Phosphoserine Ref.10
Modified residue6851Phosphothreonine Ref.5 Ref.10
Modified residue7211Phosphoserine By similarity
Modified residue7251Phosphoserine By similarity
Modified residue7821Phosphoserine By similarity
Modified residue8651Phosphothreonine Ref.8
Modified residue8681Phosphoserine Ref.8
Modified residue8791Phosphoserine Ref.8

Natural variations

Alternative sequence484 – 49512Missing in isoform 2 and isoform 3.
VSP_023964
Alternative sequence556 – 691136Missing in isoform 3.
VSP_023965

Experimental info

Sequence conflict261A → T in BAC65533. Ref.2
Sequence conflict1421F → Y in AAC68583. Ref.1
Sequence conflict1421F → Y in BAE27810. Ref.3
Sequence conflict1421F → Y in BAE32774. Ref.3
Sequence conflict4341Missing in BAE27810. Ref.3
Sequence conflict4511E → D in AAC68583. Ref.1
Sequence conflict4511E → D in BAE27810. Ref.3
Sequence conflict4511E → D in BAE32774. Ref.3
Sequence conflict5801M → T in AAC68583. Ref.1
Sequence conflict6591Q → R in AAC68583. Ref.1
Sequence conflict7081K → R in BAE27810. Ref.3

Sequences

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

Last modified March 20, 2007. Version 2.
Checksum: E5C91175FA33D067

FASTA87998,315
        10         20         30         40         50         60 
MTTETGPDSE VKKAQEETPQ QPEAAAAVTT PVTPAGHSHP ETNSNEKHLT QQDTRPAEQS 

        70         80         90        100        110        120 
LDMDDKDYSE ADGLSERTTP SKAQKSPQKI AKKFKSAICR VTLLDASEYE CEVEKHGRGQ 

       130        140        150        160        170        180 
VLFDLVCEHL NLLEKDYFGL TFCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP 

       190        200        210        220        230        240 
AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL 

       250        260        270        280        290        300 
RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML 

       310        320        330        340        350        360 
GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA 

       370        380        390        400        410        420 
KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS 

       430        440        450        460        470        480 
SSKRYTMSRS LDGAEFSRPA SVSENHDAGP EGDKREDDAE SGGRRSEAEE GEVRTPTKIK 

       490        500        510        520        530        540 
ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWDRERRLPS 

       550        560        570        580        590        600 
SPASPSPKGT PEKASERAGL REGSEEKVKP PRPRAPESDM GDEDQDQERD AVFLKDNHLA 

       610        620        630        640        650        660 
IERKCSSITV SSTSSLEAEV DFTVIGDYHG GAFEDFSRSL PELDRDKSDS ETEGLVFAQD 

       670        680        690        700        710        720 
LKGPSSQEDE SGGLEDSPDR GACSTPEMPQ FESVKAETMT VSSLAIRKKI EPEAMLQSRV 

       730        740        750        760        770        780 
SAADSTQVDG GTPMVKDFMT TPPCITTETI STTMENSLKS GKGAAAMIPG PQTVATEIRS 

       790        800        810        820        830        840 
LSPIIGKDVL TSTYGATAET LSTSTTTHVT KTVKGGFSET RIEKRIIITG DEDVDQDQAL 

       850        860        870 
ALAIKEAKLQ HPDMLVTKAV VYRETDPSPE ERDKKPQES

« Hide

Isoform 2 [UniParc].

Checksum: EB0CFD9EADDB9590
Show »

FASTA86796,853
Isoform 3 [UniParc].

Checksum: 09EA8EF42AEA6ACD
Show »

FASTA73181,960

References

« Hide 'large scale' references
[1]"A novel neuron-enriched homolog of the erythrocyte membrane cytoskeletal protein 4.1."
Walensky L.D., Blackshaw S., Liao D., Watkins C.C., Weier H.-U.G., Parra M., Huganir R.L., Conboy J.G., Mohandas N., Snyder S.H.
J. Neurosci. 19:6457-6467(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[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. expand/collapse author list , 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] (ISOFORM 3).
Strain: C57BL/6J and NOD.
[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] (ISOFORM 2).
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-685, MASS SPECTROMETRY.
Tissue: Embryonic brain.
[6]"Proteomic analysis of in vivo phosphorylated synaptic proteins."
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.
J. Biol. Chem. 280:5972-5982(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-475; SER-546; THR-550; SER-648 AND SER-650, MASS SPECTROMETRY.
Tissue: Forebrain.
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546; THR-550 AND SER-648, MASS SPECTROMETRY.
Tissue: Brain.
[8]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-865; SER-868 AND SER-879, MASS SPECTROMETRY.
Tissue: Teratocarcinoma.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-343, MASS SPECTROMETRY.
Tissue: Brain.
[10]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-650; SER-677 AND THR-685, MASS SPECTROMETRY.
Tissue: Brain cortex.
[11]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-510 AND SER-639, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF061283 mRNA. Translation: AAC68583.1.
AK122251 mRNA. Translation: BAC65533.1. Different initiation.
AK147272 mRNA. Translation: BAE27810.1.
AK154704 mRNA. Translation: BAE32774.1.
BC034751 mRNA. Translation: AAH34751.1.
IPIIPI00465812.
IPI00830613.
IPI00831205.
RefSeqNP_001003815.1. NM_001003815.2.
NP_001006665.1. NM_001006664.2.
NP_038538.1. NM_013510.3.
UniGeneMm.20852.

3D structure databases

ProteinModelPortalQ9Z2H5.
SMRQ9Z2H5. Positions 95-377.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Z2H5. 1 interaction.
STRING10090.ENSMUSP00000065040.

PTM databases

PhosphoSiteQ9Z2H5.

Proteomic databases

PaxDbQ9Z2H5.
PRIDEQ9Z2H5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13821.
KEGGmmu:13821.

Organism-specific databases

CTD13821.
MGIMGI:103010. Epb4.1l1.
RougeSearch...

Phylogenomic databases

eggNOGNOG242913.
HOGENOMHOG000228841.
HOVERGENHBG007777.
KOK06107.
OrthoDBEOG4J9MZ6.

Gene expression databases

CleanExMM_EPB4.1L1.
GenevestigatorQ9Z2H5.

Family and domain databases

Gene3D1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR008379. Band_4.1_C.
IPR019749. Band_41_domain.
IPR019750. Band_41_fam.
IPR021187. Band_41_protein.
IPR000798. Ez/rad/moesin_like.
IPR014847. FERM-adjacent.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR018980. FERM_PH-like_C.
IPR011993. PH_like_dom.
IPR007477. SAB_dom.
[Graphical view]
PfamPF05902. 4_1_CTD. 1 hit.
PF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF04382. SAB. 1 hit.
[Graphical view]
PIRSFPIRSF002304. Membrane_skeletal_4_1. 1 hit.
PRINTSPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTSM00295. B41. 1 hit.
[Graphical view]
SUPFAMSSF47031. FERM_3-hlx. 1 hit.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284612.
SOURCESearch...

Entry information

Entry nameE41L1_MOUSE
AccessionPrimary (citable) accession number: Q9Z2H5
Secondary accession number(s): Q3U3L1 expand/collapse secondary AC list , Q3UHP7, Q80U34, Q8K204
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: March 20, 2007
Last modified: May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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