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P02549

- SPTA1_HUMAN

UniProt

P02549 - SPTA1_HUMAN

Protein

Spectrin alpha chain, erythrocytic 1

Gene

SPTA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 5 (05 Oct 2010)
      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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi2284 – 2295121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi2327 – 2338122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. actin filament binding Source: ProtInc
    2. calcium ion binding Source: InterPro
    3. protein binding Source: IntAct
    4. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

    1. actin filament capping Source: UniProtKB-KW
    2. actin filament organization Source: ProtInc
    3. axon guidance Source: Reactome
    4. hemopoiesis Source: Ensembl
    5. lymphocyte homeostasis Source: Ensembl
    6. plasma membrane organization Source: Ensembl
    7. porphyrin-containing compound biosynthetic process Source: Ensembl
    8. positive regulation of protein binding Source: Ensembl
    9. positive regulation of T cell proliferation Source: Ensembl
    10. regulation of cell shape Source: UniProtKB-KW

    Keywords - Molecular functioni

    Actin capping

    Keywords - Biological processi

    Cell shape

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-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 alpha chain, erythrocytic 1
    Alternative name(s):
    Erythroid alpha-spectrin
    Gene namesi
    Name:SPTA1
    Synonyms:SPTA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11272. SPTA1.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: BHF-UCL
    2. cuticular plate Source: Ensembl
    3. cytosol Source: Reactome
    4. intrinsic component of the cytoplasmic side of the plasma membrane Source: BHF-UCL
    5. spectrin Source: ProtInc
    6. spectrin-associated cytoskeleton Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Elliptocytosis 2 (EL2) [MIM:130600]: 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.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241I → S in EL2; Lograno. 1 Publication
    VAR_001324
    Natural varianti28 – 281R → C in EL2. 1 Publication
    VAR_001328
    Natural varianti28 – 281R → H in EL2; Corbeil. 1 Publication
    Corresponds to variant rs28934004 [ dbSNP | Ensembl ].
    VAR_001325
    Natural varianti28 – 281R → L in EL2. 1 Publication
    VAR_001326
    Natural varianti28 – 281R → S in EL2. 2 Publications
    Corresponds to variant rs28934005 [ dbSNP | Ensembl ].
    VAR_001327
    Natural varianti31 – 311V → A in EL2; Marseille.
    VAR_001329
    Natural varianti34 – 341R → W in EL2; Genova. 1 Publication
    VAR_001330
    Natural varianti41 – 411R → W in EL2; Tunis. 1 Publication
    VAR_001331
    Natural varianti45 – 451R → S in EL2; Clichy. 1 Publication
    VAR_001332
    Natural varianti45 – 451R → T in EL2; Anastasia. 1 Publication
    VAR_001333
    Natural varianti46 – 461G → V in EL2; Culoz. 1 Publication
    VAR_001334
    Natural varianti49 – 491L → F in EL2; Lyon. 1 Publication
    VAR_001336
    Natural varianti151 – 1511G → D in EL2; Ponte de Sor.
    VAR_001337
    Natural varianti154 – 1541L → LL in EL2.
    VAR_001338
    Natural varianti207 – 2071L → P in EL2 and HPP; Saint-Louis. 1 Publication
    Corresponds to variant rs121918643 [ dbSNP | Ensembl ].
    VAR_001339
    Natural varianti260 – 2601L → P in EL2; Nigerian. 1 Publication
    VAR_001340
    Natural varianti261 – 2611S → P in EL2. 1 Publication
    VAR_001341
    Natural varianti469 – 4691H → P in EL2; Barcelona. 1 Publication
    VAR_001342
    Natural varianti469 – 4691Missing in EL2; Alexandria.
    VAR_001343
    Natural varianti471 – 4711Q → P in EL2. 1 Publication
    VAR_001344
    Natural varianti791 – 7911D → E in EL2; Jendouba. 1 Publication
    Corresponds to variant rs7418956 [ dbSNP | Ensembl ].
    VAR_001346
    Hereditary pyropoikilocytosis (HPP) [MIM:266140]: Autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481K → R in HPP. 1 Publication
    VAR_001335
    Natural varianti207 – 2071L → P in EL2 and HPP; Saint-Louis. 1 Publication
    Corresponds to variant rs121918643 [ dbSNP | Ensembl ].
    VAR_001339
    Spherocytosis 3 (SPH3) [MIM:270970]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH3 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Elliptocytosis, Hereditary hemolytic anemia, Pyropoikilocytosis

    Organism-specific databases

    MIMi130600. phenotype.
    266140. phenotype.
    270970. phenotype.
    Orphaneti98864. Common hereditary elliptocytosis.
    98867. Hereditary pyropoikilocytosis.
    822. Hereditary spherocytosis.
    PharmGKBiPA36101.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24192419Spectrin alpha chain, erythrocytic 1PRO_0000073452Add
    BLAST

    Proteomic databases

    MaxQBiP02549.
    PaxDbiP02549.
    PRIDEiP02549.

    PTM databases

    PhosphoSiteiP02549.

    Expressioni

    Gene expression databases

    ArrayExpressiP02549.
    BgeeiP02549.
    CleanExiHS_SPTA1.
    GenevestigatoriP02549.

    Organism-specific databases

    HPAiCAB016193.
    CAB037246.
    HPA028048.
    HPA028253.

    Interactioni

    Subunit structurei

    Composed of non-homologous chains, alpha and beta, which aggregate side-to-side in an antiparallel fashion to form dimers, tetramers, and higher polymers. Interacts with FASLG.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP02EBI-375617,EBI-375446
    SPTBN1Q010823EBI-375617,EBI-351561

    Protein-protein interaction databases

    BioGridi112586. 19 interactions.
    DIPiDIP-1020N.
    DIP-17031N.
    IntActiP02549. 12 interactions.
    MINTiMINT-7211599.
    STRINGi9606.ENSP00000357130.

    Structurei

    Secondary structure

    1
    2419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 143
    Helixi24 – 263
    Helixi27 – 304
    Helixi31 – 333
    Helixi34 – 7744
    Helixi87 – 11832
    Helixi126 – 15631

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OWANMR-A1-156[»]
    3LBXX-ray2.80A1-158[»]
    ProteinModelPortaliP02549.
    SMRiP02549. Positions 1-953, 993-1034, 1049-2264, 2267-2415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02549.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati19 – 5133Spectrin 1Add
    BLAST
    Repeati53 – 156104Spectrin 2Add
    BLAST
    Repeati158 – 262105Spectrin 3Add
    BLAST
    Repeati264 – 368105Spectrin 4Add
    BLAST
    Repeati370 – 474105Spectrin 5Add
    BLAST
    Repeati476 – 580105Spectrin 6Add
    BLAST
    Repeati582 – 685104Spectrin 7Add
    BLAST
    Repeati687 – 791105Spectrin 8Add
    BLAST
    Repeati793 – 897105Spectrin 9Add
    BLAST
    Repeati899 – 96870Spectrin 10Add
    BLAST
    Domaini977 – 103660SH3PROSITE-ProRule annotationAdd
    BLAST
    Repeati1082 – 1181100Spectrin 11Add
    BLAST
    Repeati1183 – 1287105Spectrin 12Add
    BLAST
    Repeati1289 – 1393105Spectrin 13Add
    BLAST
    Repeati1395 – 1498104Spectrin 14Add
    BLAST
    Repeati1500 – 1605106Spectrin 15Add
    BLAST
    Repeati1607 – 1711105Spectrin 16Add
    BLAST
    Repeati1713 – 1817105Spectrin 17Add
    BLAST
    Repeati1819 – 1926108Spectrin 18Add
    BLAST
    Repeati1928 – 2033106Spectrin 19Add
    BLAST
    Repeati2043 – 2147105Spectrin 20Add
    BLAST
    Repeati2157 – 2258102Spectrin 21Add
    BLAST
    Domaini2271 – 230636EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2314 – 234936EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2352 – 238635EF-hand 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the spectrin family.Curated
    Contains 3 EF-hand domains.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation
    Contains 21 spectrin repeats.Curated

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiNOG237318.
    HOGENOMiHOG000246965.
    HOVERGENiHBG059266.
    InParanoidiP02549.
    KOiK06114.
    OMAiSINKDWW.
    OrthoDBiEOG7GXP9K.
    PhylomeDBiP02549.
    TreeFamiTF343803.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR002048. EF_hand_dom.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR013315. Spectrin_alpha_SH3.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PfamiPF08726. EFhand_Ca_insen. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF00435. Spectrin. 20 hits.
    [Graphical view]
    PRINTSiPR01887. SPECTRNALPHA.
    SMARTiSM00054. EFh. 2 hits.
    SM00326. SH3. 1 hit.
    SM00150. SPEC. 20 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50222. EF_HAND_2. 3 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P02549-1) [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

    MEQFPKETVV ESSGPKVLET AEEIQERRQE VLTRYQSFKE RVAERGQKLE     50
    DSYHLQVFKR DADDLGKWIM EKVNILTDKS YEDPTNIQGK YQKHQSLEAE 100
    VQTKSRLMSE LEKTREERFT MGHSAHEETK AHIEELRHLW DLLLELTLEK 150
    GDQLLRALKF QQYVQECADI LEWIGDKEAI ATSVELGEDW ERTEVLHKKF 200
    EDFQVELVAK EGRVVEVNQY ANECAEENHP DLPLIQSKQN EVNAAWERLR 250
    GLALQRQKAL SNAANLQRFK RDVTEAIQWI KEKEPVLTSE DYGKDLVASE 300
    GLFHSHKGLE RNLAVMSDKV KELCAKAEKL TLSHPSDAPQ IQEMKEDLVS 350
    SWEHIRALAT SRYEKLQATY WYHRFSSDFD ELSGWMNEKT AAINADELPT 400
    DVAGGEVLLD RHQQHKHEID SYDDRFQSAD ETGQDLVNAN HEASDEVREK 450
    MEILDNNWTA LLELWDERHR QYEQCLDFHL FYRDSEQVDS WMSRQEAFLE 500
    NEDLGNSLGS AEALLQKHED FEEAFTAQEE KIITVDKTAT KLIGDDHYDS 550
    ENIKAIRDGL LARRDALREK AATRRRLLKE SLLLQKLYED SDDLKNWINK 600
    KKKLADDEDY KDIQNLKSRV QKQQVFEKEL AVNKTQLENI QKTGQEMIEG 650
    GHYASDNVTT RLSEVASLWE ELLEATKQKG TQLHEANQQL QFENNAEDLQ 700
    RWLEDVEWQV TSEDYGKGLA EVQNRLRKHG LLESAVAARQ DQVDILTDLA 750
    AYFEEIGHPD SKDIRARQES LVCRFEALKE PLATRKKKLL DLLHLQLICR 800
    DTEDEEAWIQ ETEPSATSTY LGKDLIASKK LLNRHRVILE NIASHEPRIQ 850
    EITERGNKMV EEGHFAAEDV ASRVKSLNQN MESLRARAAR RQNDLEANVQ 900
    FQQYLADLHE AETWIREKEP IVDNTNYGAD EEAAGALLKK HEAFLLDLNS 950
    FGDSMKALRN QANACQQQQA APVEGVAGEQ RVMALYDFQA RSPREVTMKK 1000
    GDVLTLLSSI NKDWWKVEAA DHQGIVPAVY VRRLAHDEFP MLPQRRREEP 1050
    GNITQRQEQI ENQYRSLLDR AEERRRRLLQ RYNEFLLAYE AGDMLEWIQE 1100
    KKAENTGVEL DDVWELQKKF DEFQKDLNTN EPRLRDINKV ADDLLFEGLL 1150
    TPEGAQIRQE LNSRWGSLQR LADEQRQLLG SAHAVEVFHR EADDTKEQIE 1200
    KKCQALSAAD PGSDLFSVQA LQRRHEGFER DLVPLGDKVT ILGETAERLS 1250
    ESHPDATEDL QRQKMELNEA WEDLQGRTKD RKESLNEAQK FYLFLSKARD 1300
    LQNWISSIGG MVSSQELAED LTGIEILLER HQEHRADMEA EAPTFQALED 1350
    FSAELIDSGH HASPEIEKKL QAVKLERDDL EKAWEKRKKI LDQCLELQMF 1400
    QGNCDQVESW MVARENSLRS DDKSSLDSLE ALMKKRDDLD KAITAQEGKI 1450
    TDLEHFAESL IADEHYAKEE IATRLQRVLD RWKALKAQLI DERTKLGDYA 1500
    NLKQFYRDLE ELEEWISEML PTACDESYKD ATNIQRKYLK HQTFAHEVDG 1550
    RSEQVHGVIN LGNSLIECSA CDGNEEAMKE QLEQLKEHWD HLLERTNDKG 1600
    KKLNEASRQQ RFNTSIRDFE FWLSEAETLL AMKDQARDLA SAGNLLKKHQ 1650
    LLEREMLARE DALKDLNTLA EDLLSSGTFN VDQIVKKKDN VNKRFLNVQE 1700
    LAAAHHEKLK EAYALFQFFQ DLDDEESWIE EKLIRVSSQD YGRDLQGVQN 1750
    LLKKHKRLEG ELVAHEPAIQ NVLDMAEKLK DKAAVGQEEI QLRLAQFVEH 1800
    WEKLKELAKA RGLKLEESLE YLQFMQNAEE EEAWINEKNA LAVRGDCGDT 1850
    LAATQSLLMK HEALENDFAV HETRVQNVCA QGEDILNKVL QEESQNKEIS 1900
    SKIEALNEKT PSLAKAIAAW KLQLEDDYAF QEFNWKADVV EAWIADKETS 1950
    LKTNGNGADL GDFLTLLAKQ DTLDASLQSF QQERLPEITD LKDKLISAQH 2000
    NQSKAIEERY AALLKRWEQL LEASAVHRQK LLEKQLPLQK AEDLFVEFAH 2050
    KASALNNWCE KMEENLSEPV HCVSLNEIRQ LQKDHEDFLA SLARAQADFK 2100
    CLLELDQQIK ALGVPSSPYT WLTVEVLERT WKHLSDIIEE REQELQKEEA 2150
    RQVKNFEMCQ EFEQNASTFL QWILETRAYF LDGSLLKETG TLESQLEANK 2200
    RKQKEIQAMK RQLTKIVDLG DNLEDALILD IKYSTIGLAQ QWDQLYQLGL 2250
    RMQHNLEQQI QAKDIKGVSE ETLKEFSTIY KHFDENLTGR LTHKEFRSCL 2300
    RGLNYYLPMV EEDEHEPKFE KFLDAVDPGR KGYVSLEDYT AFLIDKESEN 2350
    IKSSDEIENA FQALAEGKSY ITKEDMKQAL TPEQVSFCAT HMQQYMDPRG 2400
    RSHLSGYDYV GFTNSYFGN 2419
    Length:2,419
    Mass (Da):280,014
    Last modified:October 5, 2010 - v5
    Checksum:iB60680145C58DF55
    GO
    Isoform 2 (identifier: P02549-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1889-1891: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:2,416
    Mass (Da):279,674
    Checksum:iC3824332610EF99C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 13012Missing in AAA60575. (PubMed:2794061)CuratedAdd
    BLAST
    Sequence conflicti395 – 3951A → G in AAA60575. (PubMed:2794061)Curated
    Sequence conflicti1410 – 14101W → R in AAA60577. (PubMed:1689726)Curated
    Sequence conflicti1410 – 14101W → R in AAA60994. (PubMed:1689726)Curated
    Sequence conflicti1570 – 15701Missing in AAA60577. (PubMed:1689726)Curated
    Sequence conflicti1570 – 15701Missing in AAA60994. (PubMed:1689726)Curated
    Sequence conflicti1570 – 15701Missing in AAA60569. (PubMed:3000887)Curated
    Sequence conflicti1891 – 18911Q → H in AAA60577. (PubMed:1689726)Curated
    Sequence conflicti1891 – 18911Q → H in AAA60994. (PubMed:1689726)Curated
    Sequence conflicti2400 – 241920GRSHL…SYFGN → VEAISLAMTTLASPIPTLAT NKQLLVDRRKS in AAA60577. (PubMed:1689726)CuratedAdd
    BLAST
    Sequence conflicti2400 – 241920GRSHL…SYFGN → VEAISLAMTTLASPIPTLAT NKQLLVDRRKS in AAA60994. (PubMed:1689726)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241I → S in EL2; Lograno. 1 Publication
    VAR_001324
    Natural varianti28 – 281R → C in EL2. 1 Publication
    VAR_001328
    Natural varianti28 – 281R → H in EL2; Corbeil. 1 Publication
    Corresponds to variant rs28934004 [ dbSNP | Ensembl ].
    VAR_001325
    Natural varianti28 – 281R → L in EL2. 1 Publication
    VAR_001326
    Natural varianti28 – 281R → S in EL2. 2 Publications
    Corresponds to variant rs28934005 [ dbSNP | Ensembl ].
    VAR_001327
    Natural varianti31 – 311V → A in EL2; Marseille.
    VAR_001329
    Natural varianti34 – 341R → W in EL2; Genova. 1 Publication
    VAR_001330
    Natural varianti41 – 411R → W in EL2; Tunis. 1 Publication
    VAR_001331
    Natural varianti45 – 451R → S in EL2; Clichy. 1 Publication
    VAR_001332
    Natural varianti45 – 451R → T in EL2; Anastasia. 1 Publication
    VAR_001333
    Natural varianti46 – 461G → V in EL2; Culoz. 1 Publication
    VAR_001334
    Natural varianti48 – 481K → R in HPP. 1 Publication
    VAR_001335
    Natural varianti49 – 491L → F in EL2; Lyon. 1 Publication
    VAR_001336
    Natural varianti109 – 1091S → F.
    Corresponds to variant rs3737521 [ dbSNP | Ensembl ].
    VAR_038506
    Natural varianti151 – 1511G → D in EL2; Ponte de Sor.
    VAR_001337
    Natural varianti152 – 1521D → N.
    Corresponds to variant rs16840544 [ dbSNP | Ensembl ].
    VAR_038507
    Natural varianti154 – 1541L → LL in EL2.
    VAR_001338
    Natural varianti207 – 2071L → P in EL2 and HPP; Saint-Louis. 1 Publication
    Corresponds to variant rs121918643 [ dbSNP | Ensembl ].
    VAR_001339
    Natural varianti260 – 2601L → P in EL2; Nigerian. 1 Publication
    VAR_001340
    Natural varianti261 – 2611S → P in EL2. 1 Publication
    VAR_001341
    Natural varianti469 – 4691H → P in EL2; Barcelona. 1 Publication
    VAR_001342
    Natural varianti469 – 4691Missing in EL2; Alexandria.
    VAR_001343
    Natural varianti471 – 4711Q → P in EL2. 1 Publication
    VAR_001344
    Natural varianti701 – 7011R → H.
    Corresponds to variant rs12090314 [ dbSNP | Ensembl ].
    VAR_001345
    Natural varianti766 – 7661A → T.
    Corresponds to variant rs11265047 [ dbSNP | Ensembl ].
    VAR_038508
    Natural varianti791 – 7911D → E in EL2; Jendouba. 1 Publication
    Corresponds to variant rs7418956 [ dbSNP | Ensembl ].
    VAR_001346
    Natural varianti809 – 8091I → V.
    Corresponds to variant rs7547313 [ dbSNP | Ensembl ].
    VAR_001347
    Natural varianti853 – 8531T → R.
    Corresponds to variant rs35121052 [ dbSNP | Ensembl ].
    VAR_001348
    Natural varianti957 – 9571A → V.
    Corresponds to variant rs34706737 [ dbSNP | Ensembl ].
    VAR_038509
    Natural varianti970 – 9701A → D.
    Corresponds to variant rs35948326 [ dbSNP | Ensembl ].
    VAR_001349
    Natural varianti1163 – 11631S → A.1 Publication
    Corresponds to variant rs2482965 [ dbSNP | Ensembl ].
    VAR_038510
    Natural varianti1330 – 13301R → I.
    Corresponds to variant rs34214405 [ dbSNP | Ensembl ].
    VAR_038511
    Natural varianti1568 – 15681C → R.2 Publications
    Corresponds to variant rs863931 [ dbSNP | Ensembl ].
    VAR_038512
    Natural varianti1693 – 16931K → Q.
    Corresponds to variant rs857725 [ dbSNP | Ensembl ].
    VAR_059199
    Natural varianti1836 – 18361N → S.
    Corresponds to variant rs16830483 [ dbSNP | Ensembl ].
    VAR_059200
    Natural varianti1858 – 18581L → V.1 Publication
    Corresponds to variant rs3737515 [ dbSNP | Ensembl ].
    VAR_001350
    Natural varianti2025 – 20251A → G in Cagliari. 1 Publication
    VAR_001351
    Natural varianti2265 – 22651I → T.
    Corresponds to variant rs952094 [ dbSNP | Ensembl ].
    VAR_059201

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1889 – 18913Missing in isoform 2. CuratedVSP_037662

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61826
    , M61776, M61777, M61778, M61779, M61780, M61781, M61782, M61783, M61852, M61784, M61785, M61787, M61788, M61789, M61791, M61792, M61793, M61794, M61795, M61796, M61797, M61798, M61799, M61800, M61801, M61802, M61803, M61804, M61805, M61806, M61807, M61808, M61809, M61810, M61811, M61812, M61814, M61815, M61816, M61817, M61818, M61819, M61820, M61821, M61822, M61823, M61824, M61825 Genomic DNA. Translation: AAA60994.1.
    M61877 mRNA. Translation: AAA60577.1.
    AL353894 Genomic DNA. Translation: CAH73936.1.
    AL353894 Genomic DNA. Translation: CAH73937.1.
    M29994
    , M29983, M29984, M29985, M29986, M29987, M29988, M29989, M29990, M29991, M29992, M29993 Genomic DNA. Translation: AAA60575.1.
    M13233 Genomic DNA. Translation: AAA53103.1.
    M11049 mRNA. Translation: AAA60569.1.
    CCDSiCCDS41423.1. [P02549-1]
    PIRiA35716. SJHUA.
    RefSeqiNP_003117.2. NM_003126.2. [P02549-1]
    UniGeneiHs.119825.

    Genome annotation databases

    EnsembliENST00000368147; ENSP00000357129; ENSG00000163554. [P02549-1]
    GeneIDi6708.
    KEGGihsa:6708.
    UCSCiuc001fst.1. human. [P02549-1]

    Polymorphism databases

    DMDMi308153675.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61826
    , M61776 , M61777 , M61778 , M61779 , M61780 , M61781 , M61782 , M61783 , M61852 , M61784 , M61785 , M61787 , M61788 , M61789 , M61791 , M61792 , M61793 , M61794 , M61795 , M61796 , M61797 , M61798 , M61799 , M61800 , M61801 , M61802 , M61803 , M61804 , M61805 , M61806 , M61807 , M61808 , M61809 , M61810 , M61811 , M61812 , M61814 , M61815 , M61816 , M61817 , M61818 , M61819 , M61820 , M61821 , M61822 , M61823 , M61824 , M61825 Genomic DNA. Translation: AAA60994.1 .
    M61877 mRNA. Translation: AAA60577.1 .
    AL353894 Genomic DNA. Translation: CAH73936.1 .
    AL353894 Genomic DNA. Translation: CAH73937.1 .
    M29994
    , M29983 , M29984 , M29985 , M29986 , M29987 , M29988 , M29989 , M29990 , M29991 , M29992 , M29993 Genomic DNA. Translation: AAA60575.1 .
    M13233 Genomic DNA. Translation: AAA53103.1 .
    M11049 mRNA. Translation: AAA60569.1 .
    CCDSi CCDS41423.1. [P02549-1 ]
    PIRi A35716. SJHUA.
    RefSeqi NP_003117.2. NM_003126.2. [P02549-1 ]
    UniGenei Hs.119825.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OWA NMR - A 1-156 [» ]
    3LBX X-ray 2.80 A 1-158 [» ]
    ProteinModelPortali P02549.
    SMRi P02549. Positions 1-953, 993-1034, 1049-2264, 2267-2415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112586. 19 interactions.
    DIPi DIP-1020N.
    DIP-17031N.
    IntActi P02549. 12 interactions.
    MINTi MINT-7211599.
    STRINGi 9606.ENSP00000357130.

    PTM databases

    PhosphoSitei P02549.

    Polymorphism databases

    DMDMi 308153675.

    Proteomic databases

    MaxQBi P02549.
    PaxDbi P02549.
    PRIDEi P02549.

    Protocols and materials databases

    DNASUi 6708.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368147 ; ENSP00000357129 ; ENSG00000163554 . [P02549-1 ]
    GeneIDi 6708.
    KEGGi hsa:6708.
    UCSCi uc001fst.1. human. [P02549-1 ]

    Organism-specific databases

    CTDi 6708.
    GeneCardsi GC01M158580.
    H-InvDB HIX0028529.
    HGNCi HGNC:11272. SPTA1.
    HPAi CAB016193.
    CAB037246.
    HPA028048.
    HPA028253.
    MIMi 130600. phenotype.
    182860. gene.
    266140. phenotype.
    270970. phenotype.
    neXtProti NX_P02549.
    Orphaneti 98864. Common hereditary elliptocytosis.
    98867. Hereditary pyropoikilocytosis.
    822. Hereditary spherocytosis.
    PharmGKBi PA36101.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237318.
    HOGENOMi HOG000246965.
    HOVERGENi HBG059266.
    InParanoidi P02549.
    KOi K06114.
    OMAi SINKDWW.
    OrthoDBi EOG7GXP9K.
    PhylomeDBi P02549.
    TreeFami TF343803.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi SPTA1. human.
    EvolutionaryTracei P02549.
    GeneWikii Spectrin,_alpha_1.
    GenomeRNAii 6708.
    NextBioi 26158.
    PROi P02549.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02549.
    Bgeei P02549.
    CleanExi HS_SPTA1.
    Genevestigatori P02549.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR002048. EF_hand_dom.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR013315. Spectrin_alpha_SH3.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    Pfami PF08726. EFhand_Ca_insen. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF00435. Spectrin. 20 hits.
    [Graphical view ]
    PRINTSi PR01887. SPECTRNALPHA.
    SMARTi SM00054. EFh. 2 hits.
    SM00326. SH3. 1 hit.
    SM00150. SPEC. 20 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50222. EF_HAND_2. 3 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin."
      Sahr K.E., Laurila P., Kotula L., Scarpa A.L., Coupal E., Leto T.L., Linnenbach A.J., Winkelmann J.C., Speicher D.W., Marchesi V.T., Curtis P.J., Forget B.G.
      J. Biol. Chem. 265:4434-4443(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS ALA-1163 AND ARG-1568.
    2. "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].
    3. "Sequence and exon-intron organization of the DNA encoding the alpha I domain of human spectrin. Application to the study of mutations causing hereditary elliptocytosis."
      Sahr K.E., Tobe T., Scarpa A., Laughinghouse K., Marchesi S.L., Agre P., Linnenbach A.J., Marchesi V.T., Forget B.G.
      J. Clin. Invest. 84:1243-1252(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-533, VARIANTS EL2 PRO-260; PRO-261 AND PRO-471.
    4. "Structure of human erythrocyte spectrin. II. The sequence of the alpha-I domain."
      Speicher D.W., Davis G., Marchesi V.T.
      J. Biol. Chem. 258:14938-14947(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 7-601.
    5. "Structure of human erythrocyte spectrin. I. Isolation of the alpha-I domain and its cyanogen bromide peptides."
      Speicher D.W., Davis G., Yurchenco P.D., Marchesi V.T.
      J. Biol. Chem. 258:14931-14937(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 7-125.
    6. "Cloning of a portion of the chromosomal gene for human erythrocyte alpha-spectrin by using a synthetic gene fragment."
      Linnenbach A.J., Speicher D.W., Marchesi V.T., Forget B.G.
      Proc. Natl. Acad. Sci. U.S.A. 83:2397-2401(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-450.
    7. "Sequence comparison of human and murine erythrocyte alpha-spectrin cDNA."
      Curtis P.J., Palumbo A., Ming J., Fraser P.J., Cioe L., Meo P., Shane S., Rovera G.
      Gene 36:357-362(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1451-1688, VARIANT ARG-1568.
    8. "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: PARTIAL PROTEIN SEQUENCE.
    9. "Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site."
      Speicher D.W., Weglarz L., DeSilva T.M.
      J. Biol. Chem. 267:14775-14782(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 7-16; 46-55; 680-689; 1047-1056 AND 1922-1931.
    10. "The first human alpha-spectrin structural domain begins with serine."
      Lusitani D.M., Qtaishat N., LaBrake C.C., Yu R.N., Davis J., Kelley M.R., Fung L.W.-M.
      J. Biol. Chem. 269:25955-25958(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-28; 39-44 AND 50-59.
    11. Gibson T.J.
      Unpublished observations (MAR-1995)
      Cited for: IDENTIFICATION OF PROBABLE FRAMESHIFT IN 2408-2419.
    12. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structural studies on human erythrocyte alpha-spectrin tetramerization site."
      Park S., Caffrey M.S., Johnson M.E., Fung L.W.-M.
      J. Biol. Chem. 278:21837-21844(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-156, SUBUNIT.
    15. "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.
    16. "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: VARIANT EL2 SER-24.
    17. "Four different mutations in codon 28 of alpha spectrin are associated with structurally and functionally abnormal spectrin alpha I/74 in hereditary elliptocytosis."
      Coetzer T.L., Sahr K., Prchal J., Blacklock H., Peterson L., Koler R., Doyle J., Manaster J., Palek J.
      J. Clin. Invest. 88:743-749(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EL2 CYS-28; HIS-28; LEU-28 AND SER-28.
    18. "Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha I/74-kilodalton tryptic peptide."
      Floyd P.B., Gallagher P.G., Valentino L.A., Davis M., Marchesi S.L., Forget B.G.
      Blood 78:1364-1372(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2 SER-28, VARIANT HPP ARG-48.
    19. "Sp alpha I/78: a mutation of the alpha I spectrin domain in a white kindred with HE and HPP phenotypes."
      Lecomte M.-C., Garbarz M., Grandchamp B., Feo C., Gautero H., Devaux I., Bournier O., Galand C., D'Auriol L., Galibert F., Sahr K.E., Forget B.G., Boivin P., Dhermy D.
      Blood 74:1126-1133(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2 SER-45.
    20. "A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin."
      Gallagher P.G., Tse W.T., Coetzer T., Lecomte M.-C., Garbarz M., Zarkowsky H.S., Baruchel A., Ballas S.K., Dhermy D., Palek J., Forget B.G.
      J. Clin. Invest. 89:892-898(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2/HPP PRO-207.
    21. "Low expression allele alpha LELY of red cell spectrin is associated with mutations in exon 40 (alpha V/41 polymorphism) and intron 45 and with partial skipping of exon 46."
      Wilmotte R., Marechal J., Morle L., Baklouti F., Philippe N., Kastally R., Kotula L., Delaunay J., Alloisio N.
      J. Clin. Invest. 91:2091-2096(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VAL-1858.
    22. "Elliptopoikilocytosis associated with the alpha 469 His-->Pro mutation in spectrin Barcelona (alpha I/50-46b)."
      dalla Venezia N., Alloisio N., Forissier A., Denoroy L., Aymerich M., Vives-Corrons J.L., Besalduch J., Besson I., Delaunay J.
      Blood 82:1661-1665(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2 BARCELONA PRO-469.
    23. "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 CAGLIARI GLY-2025.
    24. "Two elliptocytogenic alpha I/74 variants of the spectrin alpha I domain. Spectrin Culoz (GGT-->GTT; alpha I 40 Gly-->Val) and spectrin Lyon (CTT-->TTT; alpha I 43 Leu-->Phe)."
      Morle L., Roux A.-F., Alloisio N., Pothier B., Starck J., Denoroy J., Morle F., Rudigoz R.-C., Forget B.G., Delaunay J., Godet J.
      J. Clin. Invest. 86:548-554(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2 CULOZ VAL-46, VARIANT EL2 LYON PHE-49.
    25. "Spectrin Jendouba: an alpha II/31 spectrin variant that is associated with elliptocytosis and carries a mutation distant from the dimer self-association site."
      Alloisio N., Wilmotte R., Morle L., Baklouti F., Marechal J., Ducluzeau M.-T., Denoroy L., Feo C., Forget B.G., Kastally R., Delaunay J.
      Blood 80:809-815(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2 JENDOUBA GLU-791.
    26. "Spectrin Tunis (Sp alpha I/78), an elliptocytogenic variant, is due to the CGG-->TGG codon change (Arg-->Trp) at position 35 of the alpha I domain."
      Morle L., Morle F., Roux A.-F., Godet J., Forget B.G., Denoroy L., Garbarz M., Dhermy D., Kastally R., Delaunay J.
      Blood 74:828-832(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2 TUNIS TRP-41.
    27. "Mild elliptocytosis associated with the alpha 34 Arg-->Trp mutation in spectrin Genova (alpha I/74)."
      Perrotta S., del Giudice E.M., Alloisio N., Sciarratta G., Pinto L., Delaunay J., Cutillo S., Lolascon A.
      Blood 83:3346-3349(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2 GENOVA TRP-34.
    28. "Spectrin Anastasia (alpha I/78): a new spectrin variant (alpha 45 Arg-->Thr) with moderate elliptocytogenic potential."
      Perrotta S., Iolascon A., de Angelis F., Pagano L., Colonna G., Cutillo S., del Giudice E.M.
      Br. J. Haematol. 89:933-936(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EL2 ANASTASIA THR-45.

    Entry informationi

    Entry nameiSPTA1_HUMAN
    AccessioniPrimary (citable) accession number: P02549
    Secondary accession number(s): Q15514
    , Q5VYL1, Q5VYL2, Q6LDY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 179 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 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