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P11171

- 41_HUMAN

UniProt

P11171 - 41_HUMAN

Protein

Protein 4.1

Gene

EPB41

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 4 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes.

    GO - Molecular functioni

    1. 1-phosphatidylinositol binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. spectrin binding Source: BHF-UCL
    4. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. blood circulation Source: ProtInc
    3. cortical actin cytoskeleton organization Source: InterPro
    4. positive regulation of protein binding Source: BHF-UCL

    Keywords - Ligandi

    Actin-binding, Calmodulin-binding

    Protein family/group databases

    TCDBi8.A.25.1.2. the ezrin/radixin/moesin (ezrin) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein 4.1
    Short name:
    P4.1
    Alternative name(s):
    4.1R
    Band 4.1
    EPB4.1
    Gene namesi
    Name:EPB41
    Synonyms:E41P
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3377. EPB41.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cytoplasmcell cortex 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cortical cytoskeleton Source: UniProtKB
    2. extrinsic component of membrane Source: InterPro
    3. nucleus Source: UniProtKB-SubCell
    4. plasma membrane Source: ProtInc
    5. protein complex Source: UniProtKB
    6. spectrin Source: ProtInc
    7. spectrin-associated cytoskeleton Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Elliptocytosis 1 (EL1) [MIM:611804]: A Rhesus-linked form of hereditary elliptocytosis, a genetically heterogeneous, autosomal dominant hematologic disorder. It is characterized by variable hemolytic anemia and elliptical or oval red cell shape.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Hereditary pyropoikilocytosis (HPP) [MIM:266140]: Autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi60 – 601T → A: Loss of CDK1-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-712. 1 Publication
    Mutagenesisi712 – 7121S → A: Loss of CDK1-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-60. 1 Publication

    Keywords - Diseasei

    Elliptocytosis, Hereditary hemolytic anemia, Pyropoikilocytosis

    Organism-specific databases

    MIMi266140. phenotype.
    611804. phenotype.
    Orphaneti98864. Common hereditary elliptocytosis.
    98865. Homozygous hereditary elliptocytosis.
    PharmGKBiPA27810.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 864864Protein 4.1PRO_0000219390Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei14 – 141Phosphoserine1 Publication
    Modified residuei60 – 601Phosphothreonine; by CDK11 Publication
    Modified residuei84 – 841Phosphoserine1 Publication
    Modified residuei85 – 851Phosphoserine1 Publication
    Modified residuei149 – 1491Phosphoserine1 Publication
    Modified residuei151 – 1511Phosphoserine1 Publication
    Modified residuei152 – 1521Phosphoserine1 Publication
    Modified residuei188 – 1881Phosphoserine2 Publications
    Modified residuei191 – 1911Phosphoserine1 Publication
    Modified residuei222 – 2221PhosphotyrosineBy similarity
    Modified residuei540 – 5401Phosphoserine1 Publication
    Modified residuei542 – 5421PhosphoserineBy similarity
    Modified residuei555 – 5551Phosphoserine1 Publication
    Modified residuei660 – 6601Phosphotyrosine; by EGFR1 Publication
    Modified residuei709 – 7091Phosphoserine1 Publication
    Modified residuei712 – 7121Phosphoserine; by CDK13 Publications

    Post-translational modificationi

    Phosphorylated at multiple sites by different protein kinases and each phosphorylation event selectively modulates the protein's functions.
    Phosphorylation on Tyr-660 reduces the ability of 4.1 to promote the assembly of the spectrin/actin/4.1 ternary complex.1 Publication
    O-glycosylated; contains N-acetylglucosamine side chains in the C-terminal domain.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP11171.
    PaxDbiP11171.
    PRIDEiP11171.

    PTM databases

    PhosphoSiteiP11171.
    UniCarbKBiP11171.

    Miscellaneous databases

    PMAP-CutDBB1ALH9.

    Expressioni

    Gene expression databases

    ArrayExpressiP11171.
    BgeeiP11171.
    CleanExiHS_EPB41.
    GenevestigatoriP11171.

    Organism-specific databases

    HPAiHPA028414.

    Interactioni

    Subunit structurei

    Binds with a high affinity to glycophorin and with lower affinity to band III protein. Associates with the nuclear mitotic apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate with contractile apparatus and tight junctions.

    Protein-protein interaction databases

    BioGridi108349. 24 interactions.
    DIPiDIP-17032N.
    IntActiP11171. 5 interactions.
    MINTiMINT-1208648.

    Structurei

    Secondary structure

    1
    864
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi211 – 2155
    Beta strandi221 – 2255
    Helixi232 – 24312
    Helixi248 – 2503
    Beta strandi251 – 2588
    Beta strandi261 – 2644
    Helixi271 – 2744
    Turni275 – 2773
    Beta strandi281 – 2888
    Helixi293 – 2953
    Helixi299 – 31416
    Helixi322 – 33716
    Helixi342 – 3454
    Helixi350 – 3523
    Beta strandi356 – 3583
    Helixi361 – 37212
    Helixi379 – 39012
    Turni394 – 3974
    Beta strandi399 – 4046
    Beta strandi410 – 4156
    Beta strandi417 – 4248
    Beta strandi427 – 4337
    Helixi434 – 4363
    Beta strandi437 – 4437
    Beta strandi446 – 4516
    Beta strandi454 – 4585
    Beta strandi461 – 4666
    Helixi470 – 48617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GG3X-ray2.80A/B/C210-488[»]
    2RQ1NMR-A292-396[»]
    3QIJX-ray1.80A/B211-488[»]
    DisProtiDP00678.
    ProteinModelPortaliP11171.
    SMRiP11171. Positions 208-519.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11171.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini210 – 491282FERMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni494 – 614121HydrophilicAdd
    BLAST
    Regioni615 – 71399Spectrin--actin-bindingAdd
    BLAST
    Regioni714 – 864151C-terminal (CTD)Add
    BLAST

    Sequence similaritiesi

    Contains 1 FERM domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG242913.
    HOVERGENiHBG007777.
    InParanoidiP11171.
    KOiK06107.
    OMAiHEDLTKN.
    OrthoDBiEOG7Z69BP.
    PhylomeDBiP11171.
    TreeFamiTF351626.

    Family and domain databases

    Gene3Di1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR008379. 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.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF05902. 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]
    PIRSFiPIRSF002304. Membrane_skeletal_4_1. 1 hit.
    PRINTSiPR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTiSM00295. B41. 1 hit.
    [Graphical view]
    SUPFAMiSSF47031. SSF47031. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11171-1) [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

    MTTEKSLVTE AENSQHQQKE EGEEAINSGQ QEPQQEESCQ TAAEGDNWCE    50
    QKLKASNGDT PTHEDLTKNK ERTSESRGLS RLFSSFLKRP KSQVSEEEGK 100
    EVESDKEKGE GGQKEIEFGT SLDEEIILKA PIAAPEPELK TDPSLDLHSL 150
    SSAETQPAQE ELREDPDFEI KEGEGLEECS KIEVKEESPQ SKAETELKAS 200
    QKPIRKHRNM HCKVSLLDDT VYECVVEKHA KGQDLLKRVC EHLNLLEEDY 250
    FGLAIWDNAT SKTWLDSAKE IKKQVRGVPW NFTFNVKFYP PDPAQLTEDI 300
    TRYYLCLQLR QDIVAGRLPC SFATLALLGS YTIQSELGDY DPELHGVDYV 350
    SDFKLAPNQT KELEEKVMEL HKSYRSMTPA QADLEFLENA KKLSMYGVDL 400
    HKAKDLEGVD IILGVCSSGL LVYKDKLRIN RFPWPKVLKI SYKRSSFFIK 450
    IRPGEQEQYE STIGFKLPSY RAAKKLWKVC VEHHTFFRLT STDTIPKSKF 500
    LALGSKFRYS GRTQAQTRQA SALIDRPAPH FERTASKRAS RSLDGAAAVD 550
    SADRSPRPTS APAITQGQVA EGGVLDASAK KTVVPKAQKE TVKAEVKKED 600
    EPPEQAEPEP TEAWKVEKTH IEVTVPTSNG DQTQKLAEKT EDLIRMRKKK 650
    RERLDGENIY IRHSNLMLED LDKSQEEIKK HHASISELKK NFMESVPEPR 700
    PSEWDKRLST HSPFRTLNIN GQIPTGEGPP LVKTQTVTIS DNANAVKSEI 750
    PTKDVPIVHT ETKTITYEAA QTDDNSGDLD PGVLLTAQTI TSETPSSTTT 800
    TQITKTVKGG ISETRIEKRI VITGDADIDH DQVLVQAIKE AKEQHPDMSV 850
    TKVVVHQETE IADE 864
    Length:864
    Mass (Da):97,017
    Last modified:March 7, 2006 - v4
    Checksum:iB466E7A9D7FBF12B
    GO
    Isoform 2 (identifier: P11171-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         616-648: Missing.

    Show »
    Length:831
    Mass (Da):93,239
    Checksum:iE09038E1654F9248
    GO
    Isoform 3 (identifier: P11171-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-209: Missing.
         635-648: Missing.

    Show »
    Length:641
    Mass (Da):71,955
    Checksum:i0350A4E7EF6E8AE8
    GO
    Isoform 4 (identifier: P11171-4) [UniParc]FASTAAdd to Basket

    Also known as: Erythroid

    The sequence of this isoform differs from the canonical sequence as follows:
         1-209: Missing.
         616-648: Missing.
         772-805: Missing.

    Show »
    Length:588
    Mass (Da):66,399
    Checksum:iD14399077034CFD5
    GO
    Isoform 5 (identifier: P11171-5) [UniParc]FASTAAdd to Basket

    Also known as: Non-erythroid A

    The sequence of this isoform differs from the canonical sequence as follows:
         228-262: Missing.
         616-648: Missing.
         649-669: Missing.

    Show »
    Length:775
    Mass (Da):86,603
    Checksum:i4A2D98E32CF8552C
    GO
    Isoform 6 (identifier: P11171-6) [UniParc]FASTAAdd to Basket

    Also known as: Non-erythroid B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-209: Missing.
         228-262: Missing.
         616-648: Missing.
         649-669: Missing.

    Show »
    Length:566
    Mass (Da):63,255
    Checksum:i288A47844D5CCE62
    GO
    Isoform 7 (identifier: P11171-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         635-648: Missing.
         729-734: PPLVKT → VSTLST
         735-864: Missing.

    Show »
    Length:720
    Mass (Da):81,235
    Checksum:iAE02E72F2EB18335
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511Q → H in AAD42222. 1 PublicationCurated
    Sequence conflicti76 – 761S → N in AAD42222. 1 PublicationCurated
    Sequence conflicti168 – 1681F → S in AAD42223. 1 PublicationCurated
    Sequence conflicti259 – 2591A → T in AAD42222. 1 PublicationCurated
    Sequence conflicti665 – 6651N → S in AAD42222. 1 PublicationCurated
    Sequence conflicti669 – 6691E → K no nucleotide entry (PubMed:3194408)Curated
    Sequence conflicti679 – 6791K → E in AAD42222. 1 PublicationCurated
    Sequence conflicti802 – 8021Q → K no nucleotide entry (PubMed:3223413)Curated
    Sequence conflicti802 – 8021Q → K in AAA35793. (PubMed:3375238)Curated
    Sequence conflicti802 – 8021Q → K in AAA35794. (PubMed:3375238)Curated
    Sequence conflicti852 – 8521K → L no nucleotide entry (PubMed:3194408)Curated
    Sequence conflicti863 – 8631D → E no nucleotide entry (PubMed:3194408)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141V → I.1 Publication
    Corresponds to variant rs111642750 [ dbSNP | Ensembl ].
    VAR_009122

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 209209Missing in isoform 3, isoform 4 and isoform 6. 4 PublicationsVSP_000468Add
    BLAST
    Alternative sequencei228 – 26235Missing in isoform 5 and isoform 6. 2 PublicationsVSP_000469Add
    BLAST
    Alternative sequencei616 – 64833Missing in isoform 2, isoform 4, isoform 5 and isoform 6. 3 PublicationsVSP_000470Add
    BLAST
    Alternative sequencei635 – 64814Missing in isoform 3 and isoform 7. 2 PublicationsVSP_000471Add
    BLAST
    Alternative sequencei649 – 66921Missing in isoform 5 and isoform 6. 2 PublicationsVSP_000472Add
    BLAST
    Alternative sequencei729 – 7346PPLVKT → VSTLST in isoform 7. 1 PublicationVSP_012872
    Alternative sequencei735 – 864130Missing in isoform 7. 1 PublicationVSP_012873Add
    BLAST
    Alternative sequencei772 – 80534Missing in isoform 4. 1 PublicationVSP_000473Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14993 mRNA. Translation: AAA35795.1.
    J03796 mRNA. Translation: AAA35793.1.
    J03796 mRNA. Translation: AAA35794.1.
    M61733 mRNA. Translation: AAA35797.1.
    AF156225 mRNA. Translation: AAD42222.1.
    AL138785, AL357500 Genomic DNA. Translation: CAI21967.1.
    AL138785, AL357500 Genomic DNA. Translation: CAI21966.1.
    AL138785 Genomic DNA. Translation: CAI21968.1.
    AL138785, AL357500 Genomic DNA. Translation: CAI21969.1.
    AL138785, AL357500 Genomic DNA. Translation: CAI21970.1.
    AL357500, AL138785 Genomic DNA. Translation: CAH71636.1.
    AL357500, AL138785 Genomic DNA. Translation: CAH71637.1.
    AL357500, AL138785 Genomic DNA. Translation: CAH71638.1.
    AL357500, AL138785 Genomic DNA. Translation: CAH71639.1.
    CH471059 Genomic DNA. Translation: EAX07663.1.
    CH471059 Genomic DNA. Translation: EAX07665.1.
    CH471059 Genomic DNA. Translation: EAX07667.1.
    CH471059 Genomic DNA. Translation: EAX07668.1.
    BC039079 mRNA. Translation: AAH39079.1.
    AF156226 Genomic DNA. Translation: AAD42223.1.
    CCDSiCCDS330.1. [P11171-5]
    CCDS331.1. [P11171-4]
    CCDS332.1. [P11171-3]
    CCDS53288.1. [P11171-1]
    CCDS53289.1. [P11171-7]
    PIRiA39810. MMHUE4.
    RefSeqiNP_001159477.1. NM_001166005.1. [P11171-1]
    NP_001159478.1. NM_001166006.1. [P11171-7]
    NP_004428.1. NM_004437.3. [P11171-4]
    NP_976217.1. NM_203342.2. [P11171-3]
    XP_005245818.1. XM_005245761.1. [P11171-1]
    XP_005245821.1. XM_005245764.1. [P11171-2]
    UniGeneiHs.175437.
    Hs.708933.
    Hs.712722.

    Genome annotation databases

    EnsembliENST00000343067; ENSP00000345259; ENSG00000159023. [P11171-1]
    ENST00000347529; ENSP00000290100; ENSG00000159023. [P11171-5]
    ENST00000349460; ENSP00000317597; ENSG00000159023. [P11171-3]
    ENST00000356093; ENSP00000348397; ENSG00000159023. [P11171-2]
    ENST00000373797; ENSP00000362903; ENSG00000159023. [P11171-7]
    ENST00000373798; ENSP00000362904; ENSG00000159023. [P11171-1]
    ENST00000373800; ENSP00000362906; ENSG00000159023. [P11171-4]
    GeneIDi2035.
    KEGGihsa:2035.
    UCSCiuc001brg.2. human. [P11171-3]
    uc001brh.2. human. [P11171-4]
    uc001bri.2. human. [P11171-5]
    uc001brk.3. human. [P11171-7]
    uc001brl.2. human. [P11171-2]
    uc001brm.2. human. [P11171-1]
    uc009vtm.2. human. [P11171-6]

    Polymorphism databases

    DMDMi90101808.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14993 mRNA. Translation: AAA35795.1 .
    J03796 mRNA. Translation: AAA35793.1 .
    J03796 mRNA. Translation: AAA35794.1 .
    M61733 mRNA. Translation: AAA35797.1 .
    AF156225 mRNA. Translation: AAD42222.1 .
    AL138785 , AL357500 Genomic DNA. Translation: CAI21967.1 .
    AL138785 , AL357500 Genomic DNA. Translation: CAI21966.1 .
    AL138785 Genomic DNA. Translation: CAI21968.1 .
    AL138785 , AL357500 Genomic DNA. Translation: CAI21969.1 .
    AL138785 , AL357500 Genomic DNA. Translation: CAI21970.1 .
    AL357500 , AL138785 Genomic DNA. Translation: CAH71636.1 .
    AL357500 , AL138785 Genomic DNA. Translation: CAH71637.1 .
    AL357500 , AL138785 Genomic DNA. Translation: CAH71638.1 .
    AL357500 , AL138785 Genomic DNA. Translation: CAH71639.1 .
    CH471059 Genomic DNA. Translation: EAX07663.1 .
    CH471059 Genomic DNA. Translation: EAX07665.1 .
    CH471059 Genomic DNA. Translation: EAX07667.1 .
    CH471059 Genomic DNA. Translation: EAX07668.1 .
    BC039079 mRNA. Translation: AAH39079.1 .
    AF156226 Genomic DNA. Translation: AAD42223.1 .
    CCDSi CCDS330.1. [P11171-5 ]
    CCDS331.1. [P11171-4 ]
    CCDS332.1. [P11171-3 ]
    CCDS53288.1. [P11171-1 ]
    CCDS53289.1. [P11171-7 ]
    PIRi A39810. MMHUE4.
    RefSeqi NP_001159477.1. NM_001166005.1. [P11171-1 ]
    NP_001159478.1. NM_001166006.1. [P11171-7 ]
    NP_004428.1. NM_004437.3. [P11171-4 ]
    NP_976217.1. NM_203342.2. [P11171-3 ]
    XP_005245818.1. XM_005245761.1. [P11171-1 ]
    XP_005245821.1. XM_005245764.1. [P11171-2 ]
    UniGenei Hs.175437.
    Hs.708933.
    Hs.712722.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GG3 X-ray 2.80 A/B/C 210-488 [» ]
    2RQ1 NMR - A 292-396 [» ]
    3QIJ X-ray 1.80 A/B 211-488 [» ]
    DisProti DP00678.
    ProteinModelPortali P11171.
    SMRi P11171. Positions 208-519.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108349. 24 interactions.
    DIPi DIP-17032N.
    IntActi P11171. 5 interactions.
    MINTi MINT-1208648.

    Protein family/group databases

    TCDBi 8.A.25.1.2. the ezrin/radixin/moesin (ezrin) family.

    PTM databases

    PhosphoSitei P11171.
    UniCarbKBi P11171.

    Polymorphism databases

    DMDMi 90101808.

    Proteomic databases

    MaxQBi P11171.
    PaxDbi P11171.
    PRIDEi P11171.

    Protocols and materials databases

    DNASUi 2035.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343067 ; ENSP00000345259 ; ENSG00000159023 . [P11171-1 ]
    ENST00000347529 ; ENSP00000290100 ; ENSG00000159023 . [P11171-5 ]
    ENST00000349460 ; ENSP00000317597 ; ENSG00000159023 . [P11171-3 ]
    ENST00000356093 ; ENSP00000348397 ; ENSG00000159023 . [P11171-2 ]
    ENST00000373797 ; ENSP00000362903 ; ENSG00000159023 . [P11171-7 ]
    ENST00000373798 ; ENSP00000362904 ; ENSG00000159023 . [P11171-1 ]
    ENST00000373800 ; ENSP00000362906 ; ENSG00000159023 . [P11171-4 ]
    GeneIDi 2035.
    KEGGi hsa:2035.
    UCSCi uc001brg.2. human. [P11171-3 ]
    uc001brh.2. human. [P11171-4 ]
    uc001bri.2. human. [P11171-5 ]
    uc001brk.3. human. [P11171-7 ]
    uc001brl.2. human. [P11171-2 ]
    uc001brm.2. human. [P11171-1 ]
    uc009vtm.2. human. [P11171-6 ]

    Organism-specific databases

    CTDi 2035.
    GeneCardsi GC01P029213.
    HGNCi HGNC:3377. EPB41.
    HPAi HPA028414.
    MIMi 130500. gene.
    266140. phenotype.
    611804. phenotype.
    neXtProti NX_P11171.
    Orphaneti 98864. Common hereditary elliptocytosis.
    98865. Homozygous hereditary elliptocytosis.
    PharmGKBi PA27810.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242913.
    HOVERGENi HBG007777.
    InParanoidi P11171.
    KOi K06107.
    OMAi HEDLTKN.
    OrthoDBi EOG7Z69BP.
    PhylomeDBi P11171.
    TreeFami TF351626.

    Miscellaneous databases

    ChiTaRSi EPB41. human.
    EvolutionaryTracei P11171.
    GeneWikii EPB41.
    GenomeRNAii 2035.
    NextBioi 8259.
    PMAP-CutDB B1ALH9.
    PROi P11171.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11171.
    Bgeei P11171.
    CleanExi HS_EPB41.
    Genevestigatori P11171.

    Family and domain databases

    Gene3Di 1.20.80.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR008379. 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.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF05902. 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 ]
    PIRSFi PIRSF002304. Membrane_skeletal_4_1. 1 hit.
    PRINTSi PR00935. BAND41.
    PR00661. ERMFAMILY.
    SMARTi SM00295. B41. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47031. SSF47031. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS00660. FERM_1. 1 hit.
    PS00661. FERM_2. 1 hit.
    PS50057. FERM_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton."
      Conboy J.G., Kan Y.W., Shohet S.B., Mohandas N.
      Proc. Natl. Acad. Sci. U.S.A. 83:9512-9516(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 378-393.
      Tissue: Reticulocyte.
    2. "Expression of specific isoforms of protein 4.1 in erythroid and non-erythroid tissues."
      Tang T.K., Leto T.L., Marchesi V.T., Benz E.J. Jr.
      Adv. Exp. Med. Biol. 241:81-95(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
    4. "Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1."
      Conboy J.G., Chan J.Y.C., Chasis J.A., Kan Y.W., Mohandas N.
      J. Biol. Chem. 266:8273-8280(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    5. "Sequence of protein 4.1 from a human neuroblastoma cell line: LAN5."
      Huang S.C., Wang C., Lichtenauer U., Vortmeyer A., Zhuang Z.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 7).
      Tissue: Brain.
    9. "Valine to isoleucine polymorphism in exon 4 of human protein 4.1."
      Lichtenauer U., Huang S.C., Vortmeyer A., Zhuang Z.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 157-227, VARIANT ILE-214.
    10. "Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells."
      Conboy J.G., Chan J., Mohandas N., Kan Y.W.
      Proc. Natl. Acad. Sci. U.S.A. 85:9062-9065(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 669-864 (ISOFORM 4), ALTERNATIVE SPLICING.
    11. "Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1."
      Horne W.C., Prinz W.C., Tang E.K.
      Biochim. Biophys. Acta 1055:87-92(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 534-541; 693-701 AND 793-794, PHOSPHORYLATION AT SER-540 AND SER-709.
    12. "Structure of the spectrin-actin binding site of erythrocyte protein 4.1."
      Correas I., Speicher D.W., Marchesi V.T.
      J. Biol. Chem. 261:13362-13366(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 648-714.
    13. "O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways."
      Inaba M., Maede Y.
      J. Biol. Chem. 264:18149-18155(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.
    14. "Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro."
      Subrahmanyan G., Bertics P.J., Anderson R.A.
      Proc. Natl. Acad. Sci. U.S.A. 88:5222-5226(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-660 BY EGFR.
    15. "Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1."
      Lue R.A., Marfatia S.M., Branton D., Chishti A.H.
      Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG1.
    16. "Ca(2+)-dependent and Ca(2+)-independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteins."
      Nunomura W., Takakuwa Y., Parra M., Conboy J.G., Mohandas N.
      J. Biol. Chem. 275:6360-6367(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CALMODULIN.
    17. "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex."
      Hung L.-Y., Tang C.J., Tang T.K.
      Mol. Cell. Biol. 20:7813-7825(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CENPJ.
    18. "Properties of the C-terminal domain of 4.1 proteins."
      Scott C., Phillips G.W., Baines A.J.
      Eur. J. Biochem. 268:3709-3717(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF C-TERMINAL DOMAIN.
    19. "An alternative domain containing a leucine-rich sequence regulates nuclear cytoplasmic localization of protein 4.1R."
      Luque C.M., Perez-Ferreiro C.M., Perez-Gonzalez A., Englmeier L., Koffa M.D., Correas I.
      J. Biol. Chem. 278:2686-2691(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    20. "Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 kinase."
      Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T., Jagadeeswaran R., Benz E.J. Jr.
      Mol. Biol. Cell 16:117-127(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-60 AND SER-712, PHOSPHORYLATION AT THR-60 AND SER-712.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-555 AND SER-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "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-84; SER-85; SER-188 AND SER-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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-14; SER-149; SER-151 AND SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization."
      Han B.-G., Nunomura W., Takakuwa Y., Mohandas N., Jap B.K.
      Nat. Struct. Biol. 7:871-875(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-488.

    Entry informationi

    Entry namei41_HUMAN
    AccessioniPrimary (citable) accession number: P11171
    Secondary accession number(s): B1ALH8
    , B1ALH9, D3DPM9, D3DPN0, P11176, Q14245, Q5TB35, Q5VXN8, Q8IXV9, Q9Y578, Q9Y579
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 173 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3