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Q13813

- SPTN1_HUMAN

UniProt

Q13813 - SPTN1_HUMAN

Protein

Spectrin alpha chain, non-erythrocytic 1

Gene

SPTAN1

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 3 (02 May 2006)
      Previous versions | rss
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    Functioni

    Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1176 – 11772Cleavage; by mu-calpain

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi2336 – 2347121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi2379 – 2390122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. actin filament capping Source: UniProtKB-KW
    2. apoptotic process Source: Reactome
    3. axon guidance Source: Reactome
    4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome

    Keywords - Molecular functioni

    Actin capping

    Keywords - Ligandi

    Actin-binding, Calcium, Calmodulin-binding, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    REACT_18334. NCAM signaling for neurite out-growth.
    REACT_22266. Interaction between L1 and Ankyrins.
    REACT_23832. Nephrin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Spectrin alpha chain, non-erythrocytic 1
    Alternative name(s):
    Alpha-II spectrin
    Fodrin alpha chain
    Spectrin, non-erythroid alpha subunit
    Gene namesi
    Name:SPTAN1
    Synonyms:NEAS, SPTA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11273. SPTAN1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmcell cortex
    Note: Expressed along the cell membrane in podocytes and presumptive tubule cells during glomerulogenesis and is expressed along lateral cell margins in tubule cells.By similarity

    GO - Cellular componenti

    1. cuticular plate Source: Ensembl
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. fascia adherens Source: Ensembl
    5. intracellular membrane-bounded organelle Source: HPA
    6. lateral plasma membrane Source: Ensembl
    7. membrane Source: ProtInc
    8. microtubule cytoskeleton Source: HPA
    9. spectrin Source: ProtInc
    10. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Epileptic encephalopathy, early infantile, 5 (EIEE5) [MIM:613477]: A disorder characterized by seizures associated with hypsarrhythmia, profound mental retardation with lack of visual attention and speech development, as well as spastic quadriplegia.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2202 – 22021Missing in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication
    VAR_063886
    Natural varianti2303 – 23031R → RM in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication
    VAR_063887

    Keywords - Diseasei

    Disease mutation, Epilepsy, Mental retardation

    Organism-specific databases

    MIMi613477. phenotype.
    Orphaneti1934. Early infantile epileptic encephalopathy.
    PharmGKBiPA36102.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24722472Spectrin alpha chain, non-erythrocytic 1PRO_0000073455Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei637 – 6371N6-acetyllysine1 Publication
    Modified residuei803 – 8031N6-acetyllysineBy similarity
    Modified residuei982 – 9821Phosphoserine1 Publication
    Modified residuei999 – 9991Phosphoserine1 Publication
    Modified residuei1041 – 10411Phosphoserine1 Publication
    Modified residuei1176 – 11761Phosphotyrosine1 Publication
    Modified residuei1217 – 12171Phosphoserine3 Publications
    Modified residuei1519 – 15191N6-acetyllysine1 Publication
    Modified residuei1647 – 16471Phosphoserine1 Publication
    Modified residuei2052 – 20521N6-acetyllysine1 Publication
    Modified residuei2421 – 24211N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13813.
    PaxDbiQ13813.
    PRIDEiQ13813.

    PTM databases

    PhosphoSiteiQ13813.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13813.
    BgeeiQ13813.
    GenevestigatoriQ13813.

    Organism-specific databases

    HPAiCAB004581.
    HPA007927.

    Interactioni

    Subunit structurei

    Like erythrocyte spectrin, the spectrin-like proteins are capable of forming dimers which can further associate to tetramers. Interacts (via C-terminal spectrin repeats) with TRPC4. Interacts with CALM and EMD. Interacts with isoform 1 of ACP1. Identified in a complex with ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1. Interacts with SHANK3 (via ANK repeats).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EVLQ9UI084EBI-351450,EBI-346653
    FANCGO152874EBI-351450,EBI-81610
    MLH1P406927EBI-351450,EBI-744248
    SPTBN1Q010827EBI-351450,EBI-351561

    Protein-protein interaction databases

    BioGridi112587. 114 interactions.
    DIPiDIP-33141N.
    IntActiQ13813. 47 interactions.
    MINTiMINT-4999298.

    Structurei

    Secondary structure

    1
    2472
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 2512
    Helixi30 – 6637
    Beta strandi74 – 763
    Helixi78 – 9417
    Helixi97 – 11216
    Helixi117 – 14630
    Helixi1191 – 121020
    Helixi1337 – 136226
    Beta strandi1369 – 13713
    Helixi1372 – 138918
    Helixi1392 – 140716
    Helixi1413 – 146654
    Helixi1489 – 151325
    Helixi1519 – 153921

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FOTX-ray2.45C1172-1211[»]
    3F31X-ray2.30A/B1-147[»]
    3FB2X-ray2.30A/B1337-1544[»]
    ProteinModelPortaliQ13813.
    SMRiQ13813. Positions 8-2316, 2320-2470.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13813.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati10 – 4233Spectrin 1Add
    BLAST
    Repeati44 – 147104Spectrin 2Add
    BLAST
    Repeati149 – 253105Spectrin 3Add
    BLAST
    Repeati255 – 359105Spectrin 4Add
    BLAST
    Repeati361 – 465105Spectrin 5Add
    BLAST
    Repeati467 – 571105Spectrin 6Add
    BLAST
    Repeati573 – 676104Spectrin 7Add
    BLAST
    Repeati678 – 782105Spectrin 8Add
    BLAST
    Repeati784 – 888105Spectrin 9Add
    BLAST
    Repeati890 – 95566Spectrin 10Add
    BLAST
    Domaini967 – 102660SH3PROSITE-ProRule annotationAdd
    BLAST
    Repeati1062 – 108928Spectrin 11Add
    BLAST
    Repeati1091 – 116171Spectrin 12Add
    BLAST
    Repeati1208 – 123124Spectrin 13Add
    BLAST
    Repeati1233 – 1337105Spectrin 14Add
    BLAST
    Repeati1339 – 1443105Spectrin 15Add
    BLAST
    Repeati1445 – 1549105Spectrin 16Add
    BLAST
    Repeati1551 – 1656106Spectrin 17Add
    BLAST
    Repeati1658 – 1762105Spectrin 18Add
    BLAST
    Repeati1764 – 1868105Spectrin 19Add
    BLAST
    Repeati1870 – 1974105Spectrin 20Add
    BLAST
    Repeati1976 – 2081106Spectrin 21Add
    BLAST
    Repeati2091 – 2195105Spectrin 22Add
    BLAST
    Repeati2205 – 2310106Spectrin 23Add
    BLAST
    Domaini2323 – 235836EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2366 – 240136EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2404 – 243936EF-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 23 spectrin repeats.Curated

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG5126.
    HOVERGENiHBG059266.
    KOiK06114.
    OrthoDBiEOG7GXP9K.
    PhylomeDBiQ13813.
    TreeFamiTF343803.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR013315. Spectrin_alpha_SH3.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PfamiPF13499. EF-hand_7. 1 hit.
    PF08726. EFhand_Ca_insen. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF00435. Spectrin. 20 hits.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    PR01887. SPECTRNALPHA.
    SMARTiSM00054. EFh. 2 hits.
    SM00326. SH3. 1 hit.
    SM00150. SPEC. 20 hits.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13813-1) [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

    MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ     50
    RDAEELEKWI QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV 100
    KLDETGNLMI SEGHFASETI RTRLMELHRQ WELLLEKMRE KGIKLLQAQK 150
    LVQYLRECED VMDWINDKEA IVTSEELGQD LEHVEVLQKK FEEFQTDMAA 200
    HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL KGLALQRQGK 250
    LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 300
    ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA 350
    AERHARLNDS YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL 400
    DRHQEHKGEI DAHEDSFKSA DESGQALLAA GHYASDEVRE KLTVLSEERA 450
    ALLELWELRR QQYEQCMDLQ LFYRDTEQVD NWMSKQEAFL LNEDLGDSLD 500
    SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA MEDVATRRDA 550
    LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 600
    YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA 650
    ARMNEVISLW KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH 700
    LASDDYGKDL TNVQNLQKKH ALLEADVAAH QDRIDGITIQ ARQFQDAGHF 750
    DAENIKKKQE ALVARYEALK EPMVARKQKL ADSLRLQQLF RDVEDEETWI 800
    REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI KAVTQKGNAM 850
    VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 900
    EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR 950
    EQAQSCRQQV APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST 1000
    NKDWWKVEVN DRQGFVPAAY VKKLDPAQSA SRENLLEEQG SIALRQEQID 1050
    NQTRITKEAG SVSLRMKQVE ELYHSLLELG EKRKGMLEKS CKKFMLFREA 1100
    NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL KANESRLKDI 1150
    NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH 1200
    TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE 1250
    EKNQALNTDN YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI 1300
    QSHPESAEDL QEKCTELNQA WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD 1350
    LMSWINGIRG LVSSDELAKD VTGAEALLER HQEHRTEIDA RAGTFQAFEQ 1400
    FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM LDQCLELQLF 1450
    HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 1500
    IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES 1550
    QTLQQFSRDV DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH 1600
    ANADRIRGVI DMGNSLIERG ACAGSEDAVK ARLAALADQW QFLVQKSAEK 1650
    SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL LASEDYGKDL ASVNNLLKKH 1700
    QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD TINGRFQKIK 1750
    SMAASRRAKL NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ 1800
    NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE 1850
    HWKELKQLAA ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD 1900
    TLAAIQGLLK KHEAFETDFT VHKDRVNDVC TNGQDLIKKN NHHEENISSK 1950
    MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ FNWKADVVES WIGEKENSLK 2000
    TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK DQLLAAKHVQ 2050
    SKAIEARHAS LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA 2100
    SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL 2150
    AELDRQIKSF RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ 2200
    EENDKLRQEF AQHANAFHQW IQETRTYLLD GSCMVEESGT LESQLEATKR 2250
    KHQEIRAMRS QLKKIEDLGA AMEEALILDN KYTEHSTVGL AQQWDQLDQL 2300
    GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS GRLNHQEFKS 2350
    CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET 2400
    ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD 2450
    GKGRELPTAF DYVEFTRSLF VN 2472
    Length:2,472
    Mass (Da):284,539
    Last modified:May 2, 2006 - v3
    Checksum:i4433BF74EFCEFC8A
    GO
    Isoform 2 (identifier: Q13813-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1586-1586: Q → QLSKLL

    Show »
    Length:2,477
    Mass (Da):285,094
    Checksum:i66DC2E2F50E89E1E
    GO
    Isoform 3 (identifier: Q13813-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1053-1072: Missing.

    Show »
    Length:2,452
    Mass (Da):282,282
    Checksum:iA34BBE6ADCAF5A5C
    GO

    Sequence cautioni

    The sequence BAD93097.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1501K → N in AAA51790. (PubMed:2307671)Curated
    Sequence conflicti498 – 4981S → F in AAA51790. (PubMed:2307671)Curated
    Sequence conflicti737 – 7371I → V in AAA51790. (PubMed:2307671)Curated
    Sequence conflicti737 – 7371I → V in AAA52468. (PubMed:3691949)Curated
    Sequence conflicti737 – 7371I → V in AAA51702. (PubMed:3038643)Curated
    Sequence conflicti1595 – 15951F → R in AAA52468. (PubMed:3691949)Curated
    Sequence conflicti1595 – 15951F → R in AAA51702. (PubMed:3038643)Curated
    Sequence conflicti1625 – 16251S → N in AAA51790. (PubMed:2307671)Curated
    Sequence conflicti1670 – 16712FD → IA in AAA51790. (PubMed:2307671)Curated
    Sequence conflicti1918 – 19181D → A in AAA51790. (PubMed:2307671)Curated
    Sequence conflicti1971 – 19722KL → NV in AAA51790. (PubMed:2307671)Curated
    Sequence conflicti1971 – 19722KL → NV in AAB41498. (PubMed:10625438)Curated
    Sequence conflicti2163 – 21631A → R in CAA60503. (PubMed:7607240)Curated
    Sequence conflicti2347 – 23482EF → DG in AAA51790. (PubMed:2307671)Curated
    Sequence conflicti2448 – 24481Y → I in AAA51790. (PubMed:2307671)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti385 – 3851N → S.
    Corresponds to variant rs2227863 [ dbSNP | Ensembl ].
    VAR_038513
    Natural varianti904 – 9041S → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035454
    Natural varianti1017 – 10171P → S in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035455
    Natural varianti1300 – 13001I → T.3 Publications
    Corresponds to variant rs1048236 [ dbSNP | Ensembl ].
    VAR_012227
    Natural varianti1794 – 17941R → W in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035456
    Natural varianti1918 – 19181D → N in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035457
    Natural varianti2202 – 22021Missing in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication
    VAR_063886
    Natural varianti2303 – 23031R → RM in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. 1 Publication
    VAR_063887

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1053 – 107220Missing in isoform 3. 2 PublicationsVSP_012271Add
    BLAST
    Alternative sequencei1586 – 15861Q → QLSKLL in isoform 2. 1 PublicationVSP_012270

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05243 mRNA. Translation: AAA51790.1.
    U83867 mRNA. Translation: AAB41498.1.
    AB191262 mRNA. Translation: BAD52438.1.
    AB209860 mRNA. Translation: BAD93097.1. Different initiation.
    AL356481 Genomic DNA. Translation: CAH71404.1.
    AL356481 Genomic DNA. Translation: CAH71405.1.
    BC053521 mRNA. Translation: AAH53521.1.
    M24773 mRNA. Translation: AAA52468.1.
    M18627 mRNA. Translation: AAA51702.1.
    U26396 mRNA. Translation: AAB60364.1.
    AF148808 Genomic DNA. Translation: AAF26672.1.
    X86901 mRNA. Translation: CAA60503.1.
    CCDSiCCDS48036.1. [Q13813-2]
    CCDS6905.1. [Q13813-1]
    PIRiA35715.
    RefSeqiNP_001123910.1. NM_001130438.2. [Q13813-2]
    NP_001182461.1. NM_001195532.1. [Q13813-3]
    NP_003118.2. NM_003127.3. [Q13813-1]
    UniGeneiHs.372331.

    Genome annotation databases

    EnsembliENST00000372731; ENSP00000361816; ENSG00000197694. [Q13813-1]
    ENST00000372739; ENSP00000361824; ENSG00000197694. [Q13813-2]
    GeneIDi6709.
    KEGGihsa:6709.
    UCSCiuc004bvl.4. human. [Q13813-1]
    uc004bvm.4. human. [Q13813-2]
    uc004bvn.4. human. [Q13813-3]

    Polymorphism databases

    DMDMi94730425.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05243 mRNA. Translation: AAA51790.1 .
    U83867 mRNA. Translation: AAB41498.1 .
    AB191262 mRNA. Translation: BAD52438.1 .
    AB209860 mRNA. Translation: BAD93097.1 . Different initiation.
    AL356481 Genomic DNA. Translation: CAH71404.1 .
    AL356481 Genomic DNA. Translation: CAH71405.1 .
    BC053521 mRNA. Translation: AAH53521.1 .
    M24773 mRNA. Translation: AAA52468.1 .
    M18627 mRNA. Translation: AAA51702.1 .
    U26396 mRNA. Translation: AAB60364.1 .
    AF148808 Genomic DNA. Translation: AAF26672.1 .
    X86901 mRNA. Translation: CAA60503.1 .
    CCDSi CCDS48036.1. [Q13813-2 ]
    CCDS6905.1. [Q13813-1 ]
    PIRi A35715.
    RefSeqi NP_001123910.1. NM_001130438.2. [Q13813-2 ]
    NP_001182461.1. NM_001195532.1. [Q13813-3 ]
    NP_003118.2. NM_003127.3. [Q13813-1 ]
    UniGenei Hs.372331.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FOT X-ray 2.45 C 1172-1211 [» ]
    3F31 X-ray 2.30 A/B 1-147 [» ]
    3FB2 X-ray 2.30 A/B 1337-1544 [» ]
    ProteinModelPortali Q13813.
    SMRi Q13813. Positions 8-2316, 2320-2470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112587. 114 interactions.
    DIPi DIP-33141N.
    IntActi Q13813. 47 interactions.
    MINTi MINT-4999298.

    PTM databases

    PhosphoSitei Q13813.

    Polymorphism databases

    DMDMi 94730425.

    Proteomic databases

    MaxQBi Q13813.
    PaxDbi Q13813.
    PRIDEi Q13813.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372731 ; ENSP00000361816 ; ENSG00000197694 . [Q13813-1 ]
    ENST00000372739 ; ENSP00000361824 ; ENSG00000197694 . [Q13813-2 ]
    GeneIDi 6709.
    KEGGi hsa:6709.
    UCSCi uc004bvl.4. human. [Q13813-1 ]
    uc004bvm.4. human. [Q13813-2 ]
    uc004bvn.4. human. [Q13813-3 ]

    Organism-specific databases

    CTDi 6709.
    GeneCardsi GC09P131314.
    HGNCi HGNC:11273. SPTAN1.
    HPAi CAB004581.
    HPA007927.
    MIMi 182810. gene.
    613477. phenotype.
    neXtProti NX_Q13813.
    Orphaneti 1934. Early infantile epileptic encephalopathy.
    PharmGKBi PA36102.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5126.
    HOVERGENi HBG059266.
    KOi K06114.
    OrthoDBi EOG7GXP9K.
    PhylomeDBi Q13813.
    TreeFami TF343803.

    Enzyme and pathway databases

    Reactomei REACT_13541. Caspase-mediated cleavage of cytoskeletal proteins.
    REACT_18334. NCAM signaling for neurite out-growth.
    REACT_22266. Interaction between L1 and Ankyrins.
    REACT_23832. Nephrin interactions.

    Miscellaneous databases

    ChiTaRSi SPTAN1. human.
    EvolutionaryTracei Q13813.
    GeneWikii SPTAN1.
    GenomeRNAii 6709.
    NextBioi 26162.
    PROi Q13813.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13813.
    Bgeei Q13813.
    Genevestigatori Q13813.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR001452. SH3_domain.
    IPR018159. Spectrin/alpha-actinin.
    IPR013315. Spectrin_alpha_SH3.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    Pfami PF13499. EF-hand_7. 1 hit.
    PF08726. EFhand_Ca_insen. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF00435. Spectrin. 20 hits.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    PR01887. SPECTRNALPHA.
    SMARTi SM00054. EFh. 2 hits.
    SM00326. SH3. 1 hit.
    SM00150. SPEC. 20 hits.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin."
      Moon R.T., McMahon A.P.
      J. Biol. Chem. 265:4427-4433(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-1300.
    2. "Brain and muscle express a unique alternative transcript of alphaII spectrin."
      Cianci C.D., Zhang Z., Pradhan D., Morrow J.S.
      Biochemistry 38:15721-15730(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
      Tissue: Fetal brain.
    3. "Human full-length cDNA starting with the capped site sequence."
      Kato S.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Aorta.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 3).
      Tissue: Uterus.
    7. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 157-168; 970-981; 990-1002; 1608-1619; 2138-2155 AND 2455-2467, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    8. "Structure and evolution of a non-erythroid spectrin, human alpha-fodrin."
      McMahon A.P., Moon R.T.
      Biochem. Soc. Trans. 15:804-807(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 676-1595 (ISOFORM 1), VARIANT THR-1300.
      Tissue: Lung.
    9. "cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin."
      McMahon A.P., Giebelhaus D.H., Champion J.E., Bailes J.A., Lacey S., Carritt B., Henchman S.K., Moon R.T.
      Differentiation 34:68-78(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 676-1595 (ISOFORM 1), VARIANT THR-1300.
    10. "Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility."
      Stabach P.R., Cianci C.D., Glantz S.B., Zhang Z., Morrow J.S.
      Biochemistry 36:57-65(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 811-1529 (ISOFORMS 1/2), MUTAGENESIS.
    11. "Association and linkage analyses of the nonerythroid alpha-spectrin (SPTAN1) gene on chromosome 9q34 with a large Swedish kindred."
      Murakami N., Speed W.C., Seaman M.I., Zychowski R.L., Wetterberg L., Pakstis A.J., Kidd J.R., Kidd K.K.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1073-1349.
    12. "Cloning, expression and characterization of two putative calcium-binding sites in human non-erythroid alpha-spectrin."
      Lundberg S., Bjoerk J., Loefvenberg L., Backman L.
      Eur. J. Biochem. 230:658-665(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2059-2433 (ISOFORMS 1/2/3).
      Tissue: Fetal liver.
    13. Cited for: INTERACTION WITH ACP1.
    14. "Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane."
      Holaska J.M., Kowalski A.K., Wilson K.L.
      PLoS Biol. 2:1354-1362(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EMD.
    15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels."
      Odell A.F., Van Helden D.F., Scott J.L.
      J. Biol. Chem. 283:4395-4407(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRPC4.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1041 AND TYR-1176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-637; LYS-1519; LYS-2052 AND LYS-2421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-982; SER-999; SER-1217 AND SER-1647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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-1217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "Structure of the calmodulin alphaII-spectrin complex provides insight into the regulation of cell plasticity."
      Simonovic M., Zhang Z., Cianci C.D., Steitz T.A., Morrow J.S.
      J. Biol. Chem. 281:34333-34340(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1172-1210 IN COMPLEX WITH CALM.
    26. Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-904; SER-1017; TRP-1794 AND ASN-1918.
    27. "Dominant-negative mutations in alpha-II spectrin cause West syndrome with severe cerebral hypomyelination, spastic quadriplegia, and developmental delay."
      Saitsu H., Tohyama J., Kumada T., Egawa K., Hamada K., Okada I., Mizuguchi T., Osaka H., Miyata R., Furukawa T., Haginoya K., Hoshino H., Goto T., Hachiya Y., Yamagata T., Saitoh S., Nagai T., Nishiyama K.
      , Nishimura A., Miyake N., Komada M., Hayashi K., Hirai S., Ogata K., Kato M., Fukuda A., Matsumoto N.
      Am. J. Hum. Genet. 86:881-891(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EIEE5 GLU-2202 DEL AND MET-2303 INS, CHARACTERIZATION OF VARIANTS EIEE5 GLU-2202 DEL AND MET-2303 INS.

    Entry informationi

    Entry nameiSPTN1_HUMAN
    AccessioniPrimary (citable) accession number: Q13813
    Secondary accession number(s): Q13186
    , Q15324, Q16606, Q59EF1, Q5VXV5, Q5VXV6, Q7Z6M5, Q9P0V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 162 of the entry and version 3 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 9
      Human chromosome 9: 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