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P11277

- SPTB1_HUMAN

UniProt

P11277 - SPTB1_HUMAN

Protein

Spectrin beta chain, erythrocytic

Gene

SPTB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 5 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.

    GO - Molecular functioni

    1. actin binding Source: ProtInc
    2. actin filament binding Source: UniProtKB
    3. ankyrin binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. structural constituent of cytoskeleton Source: InterPro

    GO - Biological processi

    1. actin filament capping Source: UniProtKB-KW
    2. axon guidance Source: Reactome
    3. hemopoiesis Source: Ensembl
    4. plasma membrane organization Source: Ensembl
    5. porphyrin-containing compound biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_18334. NCAM signaling for neurite out-growth.
    REACT_22266. Interaction between L1 and Ankyrins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spectrin beta chain, erythrocytic
    Alternative name(s):
    Beta-I spectrin
    Gene namesi
    Name:SPTB
    Synonyms:SPTB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:11274. SPTB.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: BHF-UCL
    2. cell surface Source: UniProtKB
    3. cytoplasm Source: HPA
    4. cytosol Source: Reactome
    5. intrinsic component of the cytoplasmic side of the plasma membrane Source: BHF-UCL
    6. protein complex Source: UniProtKB
    7. spectrin Source: ProtInc
    8. spectrin-associated cytoskeleton Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Elliptocytosis 3 (EL3) [MIM:182870]: A Rhesus-unlinked 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.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2018 – 20181A → G in EL3; Cagliary. 1 Publication
    VAR_001357
    Natural varianti2019 – 20191S → P in EL3; Providence. 1 Publication
    VAR_001358
    Natural varianti2023 – 20231A → V in EL3; Paris. 1 Publication
    VAR_001359
    Natural varianti2024 – 20241W → R in EL3; Linguere. 1 Publication
    VAR_001360
    Natural varianti2025 – 20251L → R in EL3; Buffalo.
    VAR_001361
    Natural varianti2053 – 20531A → P in EL3; Kayes. 1 Publication
    VAR_001362
    Spherocytosis 2 (SPH2) [MIM:182870]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH1 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Elliptocytosis, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi130600. phenotype.
    182870. gene+phenotype.
    Orphaneti98864. Common hereditary elliptocytosis.
    98867. Hereditary pyropoikilocytosis.
    822. Hereditary spherocytosis.
    98866. Spherocytic elliptocytosis.
    PharmGKBiPA36103.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 21372136Spectrin beta chain, erythrocyticPRO_0000073459Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2110 – 21101Phosphothreonine1 Publication
    Modified residuei2114 – 21141Phosphoserine1 Publication
    Modified residuei2117 – 21171Phosphoserine1 Publication
    Modified residuei2123 – 21231Phosphoserine1 Publication
    Modified residuei2125 – 21251Phosphoserine1 Publication
    Modified residuei2128 – 21281Phosphoserine1 Publication

    Post-translational modificationi

    The first phosphorylation event occurs on Ser-2114, followed by Ser-2125, Ser-2123, Ser-2128, Ser-2117, and Thr-2110.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP11277.
    PaxDbiP11277.
    PRIDEiP11277.

    2D gel databases

    SWISS-2DPAGEP11277.

    PTM databases

    PhosphoSiteiP11277.

    Expressioni

    Gene expression databases

    ArrayExpressiP11277.
    BgeeiP11277.
    CleanExiHS_SPTB.
    GenevestigatoriP11277.

    Organism-specific databases

    HPAiCAB015169.
    HPA003394.
    HPA003398.

    Interactioni

    Subunit structurei

    Composed of nonhomologous chains, alpha and beta, which aggregate to form dimers, tetramers, and higher polymers.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SNAPINO952953EBI-514908,EBI-296723

    Protein-protein interaction databases

    BioGridi112588. 10 interactions.
    DIPiDIP-1021N.
    IntActiP11277. 6 interactions.
    MINTiMINT-3007632.
    STRINGi9606.ENSP00000374372.

    Structurei

    Secondary structure

    1
    2137
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1065 – 108521
    Helixi1093 – 112836
    Helixi1134 – 119259
    Helixi1200 – 123637
    Helixi1242 – 127130
    Helixi1586 – 160520
    Helixi1616 – 165237
    Helixi1692 – 171322
    Helixi1722 – 175938
    Helixi1765 – 181854
    Helixi1838 – 186326
    Helixi1868 – 189124
    Helixi1902 – 192827
    Beta strandi1936 – 19383
    Helixi1941 – 197131
    Helixi1977 – 203357
    Helixi2041 – 206020
    Helixi2062 – 20698
    Helixi2073 – 208210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S35X-ray2.40A1063-1275[»]
    3EDUX-ray2.10A1692-1907[»]
    3F57X-ray2.90A/B1686-1907[»]
    3KBTX-ray2.75A/B1583-1906[»]
    3KBUX-ray2.75A/B1583-1906[»]
    3LBXX-ray2.80B1902-2084[»]
    ProteinModelPortaliP11277.
    SMRiP11277. Positions 48-280, 299-2083.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11277.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 275274Actin-bindingAdd
    BLAST
    Domaini54 – 158105CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 275103CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati276 – 384109Spectrin 1Add
    BLAST
    Repeati385 – 498114Spectrin 2Add
    BLAST
    Repeati499 – 607109Spectrin 3Add
    BLAST
    Repeati608 – 713106Spectrin 4Add
    BLAST
    Repeati714 – 818105Spectrin 5Add
    BLAST
    Repeati819 – 924106Spectrin 6Add
    BLAST
    Repeati925 – 1031107Spectrin 7Add
    BLAST
    Repeati1032 – 1138107Spectrin 8Add
    BLAST
    Repeati1139 – 1244106Spectrin 9Add
    BLAST
    Repeati1245 – 1349105Spectrin 10Add
    BLAST
    Repeati1350 – 1455106Spectrin 11Add
    BLAST
    Repeati1456 – 155499Spectrin 12Add
    BLAST
    Repeati1555 – 1660106Spectrin 13Add
    BLAST
    Repeati1661 – 1767107Spectrin 14Add
    BLAST
    Repeati1768 – 1873106Spectrin 15Add
    BLAST
    Repeati1874 – 1979106Spectrin 16Add
    BLAST
    Repeati1980 – 2085106Spectrin 17Add
    BLAST

    Sequence similaritiesi

    Belongs to the spectrin family.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 17 spectrin repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5069.
    HOGENOMiHOG000007281.
    HOVERGENiHBG057912.
    KOiK06115.
    OMAiESFHRVH.
    PhylomeDBiP11277.
    TreeFamiTF313446.

    Family and domain databases

    Gene3Di1.10.418.10. 2 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR016343. Spectrin_bsu.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PfamiPF00307. CH. 2 hits.
    PF00435. Spectrin. 17 hits.
    [Graphical view]
    PIRSFiPIRSF002297. Spectrin_beta_subunit. 1 hit.
    SMARTiSM00033. CH. 2 hits.
    SM00150. SPEC. 17 hits.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    PROSITEiPS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11277-1) [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

    MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD     50
    EREVVQKKTF TKWVNSHLAR VSCRITDLYK DLRDGRMLIK LLEVLSGEML 100
    PKPTKGKMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI 150
    WTIILRFQIQ DIVVQTQEGR ETRSAKDALL LWCQMKTAGY PHVNVTNFTS 200
    SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFNV AERQLGIIPL 250
    LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET 300
    EKMIEKYSGL ASDLLTWIEQ TITVLNSRKF ANSLTGVQQQ LQAFSTYRTV 350
    EKPPKFQEKG NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE 400
    EAEYRRELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVAQDNF 450
    GYDLAAVEAA KKKHEAIETD TAAYEERVRA LEDLAQELEK ENYHDQKRIT 500
    ARKDNILRLW SYLQELLQSR RQRLETTLAL QKLFQDMLHS IDWMDEIKAH 550
    LLSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVKAITAA TLKFTEGKGY 600
    QPCDPQVIQD RISHLEQCFE ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE 650
    SWIKEKEQIY SSLDYGKDLT SVLILQRKHK AFEDELRGLD AHLEQIFQEA 700
    HGMVARKQFG HPQIEARIKE VSAQWDQLKD LAAFCKKNLQ DAENFFQFQG 750
    DADDLKAWLQ DAHRLLSGED VGQDEGATRA LGKKHKDFLE ELEESRGVME 800
    HLEQQAQGFP EEFRDSPDVT HRLQALRELY QQVVAQADLR QQRLQEALDL 850
    YTVFGETDAC ELWMGEKEKW LAEMEMPDTL EDLEVVQHRF DILDQEMKTL 900
    MTQIDGVNLA ANSLVESGHP RSREVKQYQD HLNTRWQAFQ TLVSERREAV 950
    DSALRVHNYC VDCEETSKWI TDKTKVVEST KDLGRDLAGI IAIQRKLSGL 1000
    ERDVAAIQAR VDALERESQQ LMDSHPEQKE DIGQRQKHLE ELWQGLQQSL 1050
    QGQEDLLGEV SQLQAFLQDL DDFQAWLSIT QKAVASEDMP ESLPEAEQLL 1100
    QQHAGIKDEI DGHQDSYQRV KESGEKVIQG QTDPEYLLLG QRLEGLDTGW 1150
    NALGRMWESR SHTLAQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL 1200
    EAAEAGIRKF EDFLGSMENN RDKVLSPVDS GNKLVAEGNL YSDKIKEKVQ 1250
    LIEDRHRKNN EKAQEASVLL RDNLELQNFL QNCQELTLWI NDKLLTSQDV 1300
    SYDEARNLHN KWLKHQAFVA ELASHEGWLE NIDAEGKQLM DEKPQFTALV 1350
    SQKLEALHRL WDELQATTKE KTQHLSAARS SDLRLQTHAD LNKWISAMED 1400
    QLRSDDPGKD LTSVNRMLAK LKRVEDQVNV RKEELGELFA QVPSMGEEGG 1450
    DADLSIEKRF LDLLEPLGRR KKQLESSRAK LQISRDLEDE TLWVEERLPL 1500
    AQSADYGTNL QTVQLFMKKN QTLQNEILGH TPRVEDVLQR GQQLVEAAEI 1550
    DCQDLEERLG HLQSSWDRLR EAAAGRLQRL RDANEAQQYY LDADEAEAWI 1600
    GEQELYVISD EIPKDEEGAI VMLKRHLRQQ RAVEDYGRNI KQLASRAQGL 1650
    LSAGHPEGEQ IIRLQGQVDK HYAGLKDVAE ERKRKLENMY HLFQLKRETD 1700
    DLEQWISEKE LVASSPEMGQ DFDHVTLLRD KFRDFARETG AIGQERVDNV 1750
    NAFIERLIDA GHSEAATIAE WKDGLNEMWA DLLELIDTRM QLLAASYDLH 1800
    RYFYTGAEIL GLIDEKHREL PEDVGLDAST AESFHRVHTA FERELHLLGV 1850
    QVQQFQDVAT RLQTAYAGEK AEAIQNKEQE VSAAWQALLD ACAGRRTQLV 1900
    DTADKFRFFS MARDLLSWME SIIRQIETQE RPRDVSSVEL LMKYHQGINA 1950
    EIETRSKNFS ACLELGESLL QRQHQASEEI REKLQQVMSR RKEMNEKWEA 2000
    RWERLRMLLE VCQFSRDASV AEAWLIAQEP YLASGDFGHT VDSVEKLIKR 2050
    HEAFEKSTAS WAERFAALEK PTTLELKERQ IAERPAEETG PQEEEGETAG 2100
    EAPVSHHAAT ERTSPVSLWS RLSSSWESLQ PEPSHPY 2137
    Length:2,137
    Mass (Da):246,468
    Last modified:November 25, 2008 - v5
    Checksum:i311AE5CD53237610
    GO
    Isoform 2 (identifier: P11277-2) [UniParc]FASTAAdd to Basket

    Also known as: Muscle-specific

    The sequence of this isoform differs from the canonical sequence as follows:
         2116-2137: VSLWSRLSSSWESLQPEPSHPY → GEEEGTWPQN...KRFSFFPKKK

    Show »
    Length:2,328
    Mass (Da):267,826
    Checksum:i5C3709E99F70B8D0
    GO
    Isoform 3 (identifier: P11277-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2074-2137: LELKERQIAE...SLQPEPSHPY → ASRGGRRDSRGGSSFPPCGHRENVPGQSLVSFV

    Note: Due to exon skipping.

    Show »
    Length:2,106
    Mass (Da):242,802
    Checksum:iE48305033176AE98
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti403 – 4031E → G in AAA60578. (PubMed:2195026)Curated
    Sequence conflicti403 – 4031E → G in AAA60579. (PubMed:2195026)Curated
    Sequence conflicti612 – 6121I → M in AAA60578. (PubMed:2195026)Curated
    Sequence conflicti612 – 6121I → M in AAA60579. (PubMed:2195026)Curated
    Sequence conflicti629 – 6313RKA → ART in AAA60578. (PubMed:2195026)Curated
    Sequence conflicti629 – 6313RKA → ART in AAA60579. (PubMed:2195026)Curated
    Sequence conflicti958 – 9592NY → TL in AAA60578. (PubMed:2195026)Curated
    Sequence conflicti958 – 9592NY → TL in AAA60579. (PubMed:2195026)Curated
    Sequence conflicti1031 – 10311D → N in AAA60578. (PubMed:2195026)Curated
    Sequence conflicti1031 – 10311D → N in AAA60579. (PubMed:2195026)Curated
    Sequence conflicti1844 – 18452EL → DV in AAA60578. (PubMed:2195026)Curated
    Sequence conflicti1844 – 18452EL → DV in AAA60579. (PubMed:2195026)Curated
    Sequence conflicti1844 – 18452EL → DV in AAA63259. (PubMed:2056132)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti202 – 2021W → R in HS; Kissimmee. 1 Publication
    VAR_001352
    Natural varianti439 – 4391S → N.1 Publication
    Corresponds to variant rs229587 [ dbSNP | Ensembl ].
    VAR_001353
    Natural varianti525 – 5251E → K.
    Corresponds to variant rs55752508 [ dbSNP | Ensembl ].
    VAR_061084
    Natural varianti613 – 6131S → I.
    Corresponds to variant rs3742601 [ dbSNP | Ensembl ].
    VAR_038514
    Natural varianti1151 – 11511N → D.3 Publications
    Corresponds to variant rs77806 [ dbSNP | Ensembl ].
    VAR_001354
    Natural varianti1374 – 13741H → R.1 Publication
    Corresponds to variant rs10132778 [ dbSNP | Ensembl ].
    VAR_001355
    Natural varianti1403 – 14031R → Q.
    Corresponds to variant rs17180350 [ dbSNP | Ensembl ].
    VAR_001356
    Natural varianti1408 – 14081G → R.
    Corresponds to variant rs17245552 [ dbSNP | Ensembl ].
    VAR_038515
    Natural varianti2018 – 20181A → G in EL3; Cagliary. 1 Publication
    VAR_001357
    Natural varianti2019 – 20191S → P in EL3; Providence. 1 Publication
    VAR_001358
    Natural varianti2023 – 20231A → V in EL3; Paris. 1 Publication
    VAR_001359
    Natural varianti2024 – 20241W → R in EL3; Linguere. 1 Publication
    VAR_001360
    Natural varianti2025 – 20251L → R in EL3; Buffalo.
    VAR_001361
    Natural varianti2053 – 20531A → P in EL3; Kayes. 1 Publication
    VAR_001362

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2074 – 213764LELKE…PSHPY → ASRGGRRDSRGGSSFPPCGH RENVPGQSLVSFV in isoform 3. 1 PublicationVSP_007242Add
    BLAST
    Alternative sequencei2116 – 213722VSLWS…PSHPY → GEEEGTWPQNLQQPPPPGQH KDGQKSTGDERPTTEPLFKV LDTPLSEGDEPATLPAPRDH GQSVQMEGYLGRKHDLEGPN KKASNRSWNNLYCVLRNSEL TFYKDAKNLALGMPYHGEEP LALRHAICEIAANYKKKKHV FKLRLSNGSEWLFHGKDEEE MLSWLQGVSTAINESQSIRV KAQSLPLPSLSGPDASLGKK DKEKRFSFFPKKK in isoform 2. 1 PublicationVSP_000719Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05500 mRNA. Translation: AAA60578.1.
    J05500 mRNA. Translation: AAA60579.1.
    AL121774 Genomic DNA. No translation available.
    M37884 mRNA. Translation: AAA63259.1.
    M37885 mRNA. Translation: AAA60571.1.
    M57948 mRNA. No translation available.
    X59510 mRNA. Translation: CAA42097.1.
    X59511 mRNA. Translation: CAA42098.1.
    M18054 mRNA. Translation: AAA60572.1.
    CCDSiCCDS32099.1. [P11277-2]
    CCDS32100.1. [P11277-1]
    PIRiA37064. SJHUB.
    RefSeqiNP_000338.3. NM_000347.5. [P11277-1]
    NP_001020029.1. NM_001024858.2. [P11277-2]
    XP_005268080.1. XM_005268023.2. [P11277-2]
    XP_006720304.1. XM_006720241.1. [P11277-2]
    UniGeneiHs.417303.

    Genome annotation databases

    EnsembliENST00000389720; ENSP00000374370; ENSG00000070182. [P11277-3]
    ENST00000389721; ENSP00000374371; ENSG00000070182. [P11277-1]
    ENST00000389722; ENSP00000374372; ENSG00000070182. [P11277-2]
    ENST00000556626; ENSP00000451752; ENSG00000070182. [P11277-2]
    GeneIDi6710.
    KEGGihsa:6710.
    UCSCiuc001xhr.3. human. [P11277-2]
    uc001xht.3. human. [P11277-1]

    Polymorphism databases

    DMDMi215274269.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05500 mRNA. Translation: AAA60578.1 .
    J05500 mRNA. Translation: AAA60579.1 .
    AL121774 Genomic DNA. No translation available.
    M37884 mRNA. Translation: AAA63259.1 .
    M37885 mRNA. Translation: AAA60571.1 .
    M57948 mRNA. No translation available.
    X59510 mRNA. Translation: CAA42097.1 .
    X59511 mRNA. Translation: CAA42098.1 .
    M18054 mRNA. Translation: AAA60572.1 .
    CCDSi CCDS32099.1. [P11277-2 ]
    CCDS32100.1. [P11277-1 ]
    PIRi A37064. SJHUB.
    RefSeqi NP_000338.3. NM_000347.5. [P11277-1 ]
    NP_001020029.1. NM_001024858.2. [P11277-2 ]
    XP_005268080.1. XM_005268023.2. [P11277-2 ]
    XP_006720304.1. XM_006720241.1. [P11277-2 ]
    UniGenei Hs.417303.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S35 X-ray 2.40 A 1063-1275 [» ]
    3EDU X-ray 2.10 A 1692-1907 [» ]
    3F57 X-ray 2.90 A/B 1686-1907 [» ]
    3KBT X-ray 2.75 A/B 1583-1906 [» ]
    3KBU X-ray 2.75 A/B 1583-1906 [» ]
    3LBX X-ray 2.80 B 1902-2084 [» ]
    ProteinModelPortali P11277.
    SMRi P11277. Positions 48-280, 299-2083.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112588. 10 interactions.
    DIPi DIP-1021N.
    IntActi P11277. 6 interactions.
    MINTi MINT-3007632.
    STRINGi 9606.ENSP00000374372.

    PTM databases

    PhosphoSitei P11277.

    Polymorphism databases

    DMDMi 215274269.

    2D gel databases

    SWISS-2DPAGE P11277.

    Proteomic databases

    MaxQBi P11277.
    PaxDbi P11277.
    PRIDEi P11277.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389720 ; ENSP00000374370 ; ENSG00000070182 . [P11277-3 ]
    ENST00000389721 ; ENSP00000374371 ; ENSG00000070182 . [P11277-1 ]
    ENST00000389722 ; ENSP00000374372 ; ENSG00000070182 . [P11277-2 ]
    ENST00000556626 ; ENSP00000451752 ; ENSG00000070182 . [P11277-2 ]
    GeneIDi 6710.
    KEGGi hsa:6710.
    UCSCi uc001xhr.3. human. [P11277-2 ]
    uc001xht.3. human. [P11277-1 ]

    Organism-specific databases

    CTDi 6710.
    GeneCardsi GC14M065213.
    HGNCi HGNC:11274. SPTB.
    HPAi CAB015169.
    HPA003394.
    HPA003398.
    MIMi 130600. phenotype.
    182870. gene+phenotype.
    neXtProti NX_P11277.
    Orphaneti 98864. Common hereditary elliptocytosis.
    98867. Hereditary pyropoikilocytosis.
    822. Hereditary spherocytosis.
    98866. Spherocytic elliptocytosis.
    PharmGKBi PA36103.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000007281.
    HOVERGENi HBG057912.
    KOi K06115.
    OMAi ESFHRVH.
    PhylomeDBi P11277.
    TreeFami TF313446.

    Enzyme and pathway databases

    Reactomei REACT_18334. NCAM signaling for neurite out-growth.
    REACT_22266. Interaction between L1 and Ankyrins.

    Miscellaneous databases

    EvolutionaryTracei P11277.
    GeneWikii SPTB.
    GenomeRNAii 6710.
    NextBioi 26166.
    PROi P11277.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11277.
    Bgeei P11277.
    CleanExi HS_SPTB.
    Genevestigatori P11277.

    Family and domain databases

    Gene3Di 1.10.418.10. 2 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR016343. Spectrin_bsu.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    PF00435. Spectrin. 17 hits.
    [Graphical view ]
    PIRSFi PIRSF002297. Spectrin_beta_subunit. 1 hit.
    SMARTi SM00033. CH. 2 hits.
    SM00150. SPEC. 17 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    PROSITEi PS00019. ACTININ_1. 1 hit.
    PS00020. ACTININ_2. 1 hit.
    PS50021. CH. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Full-length sequence of the cDNA for human erythroid beta-spectrin."
      Winkelmann J.C., Chang J.G., Tse W.T., Scarpa A.L., Marchesi V.T., Forget B.G.
      J. Biol. Chem. 265:11827-11832(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANTS ASN-439 AND ASP-1151.
    2. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation."
      Garbarz M., Tse W.T., Gallagher P.G., Picat C., Lecomte M.C., Galibert F., Dhermy D., Forget B.G.
      J. Clin. Invest. 88:76-81(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING.
    4. "Beta spectrin in human skeletal muscle. Tissue-specific differential processing of 3' beta spectrin pre-mRNA generates a beta spectrin isoform with a unique carboxyl terminus."
      Winkelmann J.C., Costa F.F., Linzie B.L., Forget B.G.
      J. Biol. Chem. 265:20449-20454(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1055-2137 (ISOFORM 2), VARIANT ASP-1151.
      Tissue: Skeletal muscle.
    5. "A splice site mutation of the beta-spectrin gene causing exon skipping in hereditary elliptocytosis associated with a truncated beta-spectrin chain."
      Gallagher P.G., Tse W.T., Costa F., Scarpa A., Boivin P., Delaunay J., Forget B.G.
      J. Biol. Chem. 266:15154-15159(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2002-2137 (ISOFORM 1).
    6. "Identification of an unusual deletion within homologous repeats of human reticulocyte beta-spectrin and probable peptide polymorphism."
      Yoon S.H., Kentros C.G., Prchal J.T.
      Gene 91:297-302(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 928-1756 (ISOFORMS 1/2/3), VARIANT ASP-1151.
    7. "Molecular cloning of the cDNA for human erythrocyte beta-spectrin."
      Winkelmann J.C., Leto T.L., Watkins P.C., Eddy R., Shows T.B., Linnenbach A.J., Sahr K.E., Kathuria N., Marchesi V.T., Forget B.G.
      Blood 72:328-334(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1334-1432 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE [MRNA] OF 1909-2137 (ISOFORM 1), VARIANT ARG-1374.
    8. "Isolation and characterization of cDNA clones for human erythrocyte beta-spectrin."
      Prchal J.T., Morley B.J., Yoon S.-H., Coetzer T.L., Palek J., Conboy J.G., Kan Y.W.
      Proc. Natl. Acad. Sci. U.S.A. 84:7468-7472(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1209-1482 (ISOFORMS 1/2/3).
    9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-18.
      Tissue: Platelet.
    10. "Erythrocyte spectrin is comprised of many homologous triple helical segments."
      Speicher D.W., Marchesi V.T.
      Nature 311:177-180(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS.
    11. "In vivo phosphorylation of human erythrocyte spectrin occurs in a sequential manner."
      Tang H.Y., Speicher D.W.
      Biochemistry 43:4251-4262(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-2110; SER-2114; SER-2117; SER-2123; SER-2125 AND SER-2128.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structural insights into the stability and flexibility of unusual erythroid spectrin repeats."
      Kusunoki H., MacDonald R.I., Mondragon A.
      Structure 12:645-656(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1064-1275.
    14. "Spectrin mutations in hereditary elliptocytosis and hereditary spherocytosis."
      Maillet P., Alloisio N., Morle L., Delaunay J.
      Hum. Mutat. 8:97-107(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    15. "Spectrin Cagliari: an Ala-->Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer."
      Sahr K.E., Coetzer T.L., Moy L.S., Derick L.H., Chishti A.H., Jarolim P., Lorenzo F., del Giudice E.M., Iolascon A., Gallanello R., Cao A., Delaunay J., Liu S.-C., Palek J.
      J. Biol. Chem. 268:22656-22662(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL3 CAGLIARI GLY-2018.
    16. "Beta spectrin Kissimmee: a spectrin variant associated with autosomal dominant hereditary spherocytosis and defective binding to protein 4.1."
      Becker P.S., Tse W.T., Lux S.E., Forget B.G.
      J. Clin. Invest. 92:612-616(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HS KISSIMMEE ARG-202.
    17. "Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene."
      Gallagher P.G., Weed S.A., Tse W.T., Benoit L., Morrow J.S., Marchesi S.L., Mohandas N., Forget B.G.
      J. Clin. Invest. 95:1174-1182(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL3 PROVIDENCE PRO-2019.
    18. "Identification of three novel spectrin alpha I/74 mutations in hereditary elliptocytosis: further support for a triple-stranded folding unit model of the spectrin heterodimer contact site."
      Parquet N., Devaux I., Boulanger L., Galand C., Boivin P., Lecomte M.-C., Dhermy D., Garbarz M.
      Blood 84:303-308(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EL3 VAL-2023 AND ARG-2024.
    19. "Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association."
      Tse W.T., Lecomte M.-C., Costa F.F., Garbarz M., Feo C., Boivin P., Dhermy D., Forget B.G.
      J. Clin. Invest. 86:909-916(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL3 PRO-2053.

    Entry informationi

    Entry nameiSPTB1_HUMAN
    AccessioniPrimary (citable) accession number: P11277
    Secondary accession number(s): Q15510, Q15519
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 162 of the entry and version 5 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

    Miscellaneous

    This complex is anchored to the cytoplasmic face of the plasma membrane via another protein, ankyrin, which binds to beta-spectrin and mediates the binding of the whole complex to a transmembrane protein band 3. The interaction of erythrocyte spectrin with other proteins through specific binding domains lead to the formation of an extensive subplasmalemmal meshwork which is thought to be responsible for the maintenance of the biconcave shape of human erythrocytes, for the regulation of plasma membrane components and for the maintenance of the lipid asymmetry of the plasma membrane.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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