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Q13813 (SPTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spectrin alpha chain, non-erythrocytic 1
Alternative name(s):
Alpha-II spectrin
Fodrin alpha chain
Spectrin, non-erythroid alpha subunit
Gene names
Name:SPTAN1
Synonyms:NEAS, SPTA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2472 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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). Ref.14 Ref.15 Ref.17

Subcellular location

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.

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28

Sequence similarities

Belongs to the spectrin family.

Contains 3 EF-hand domains.

Contains 1 SH3 domain.

Contains 23 spectrin repeats.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Epilepsy
Mental retardation
   DomainRepeat
SH3 domain
   LigandActin-binding
Calcium
Calmodulin-binding
Metal-binding
   Molecular functionActin capping
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

cuticular plate

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

fascia adherens

Inferred from electronic annotation. Source: Ensembl

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Traceable author statement Ref.1. Source: ProtInc

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

spectrin

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionactin binding

Traceable author statement Ref.1. Source: ProtInc

calcium ion binding

Inferred from electronic annotation. Source: InterPro

structural constituent of cytoskeleton

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13813-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13813-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1586-1586: Q → QLSKLL
Isoform 3 (identifier: Q13813-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24722472Spectrin alpha chain, non-erythrocytic 1
PRO_0000073455

Regions

Repeat10 – 4233Spectrin 1
Repeat44 – 147104Spectrin 2
Repeat149 – 253105Spectrin 3
Repeat255 – 359105Spectrin 4
Repeat361 – 465105Spectrin 5
Repeat467 – 571105Spectrin 6
Repeat573 – 676104Spectrin 7
Repeat678 – 782105Spectrin 8
Repeat784 – 888105Spectrin 9
Repeat890 – 95566Spectrin 10
Domain967 – 102660SH3
Repeat1062 – 108928Spectrin 11
Repeat1091 – 116171Spectrin 12
Repeat1208 – 123124Spectrin 13
Repeat1233 – 1337105Spectrin 14
Repeat1339 – 1443105Spectrin 15
Repeat1445 – 1549105Spectrin 16
Repeat1551 – 1656106Spectrin 17
Repeat1658 – 1762105Spectrin 18
Repeat1764 – 1868105Spectrin 19
Repeat1870 – 1974105Spectrin 20
Repeat1976 – 2081106Spectrin 21
Repeat2091 – 2195105Spectrin 22
Repeat2205 – 2310106Spectrin 23
Domain2323 – 235836EF-hand 1
Domain2366 – 240136EF-hand 2
Domain2404 – 243936EF-hand 3
Calcium binding2336 – 2347121 Potential
Calcium binding2379 – 2390122 Potential

Sites

Site1176 – 11772Cleavage; by mu-calpain

Amino acid modifications

Modified residue11N-acetylmethionine Ref.25
Modified residue6371N6-acetyllysine Ref.21
Modified residue8031N6-acetyllysine By similarity
Modified residue9821Phosphoserine Ref.22
Modified residue9991Phosphoserine Ref.22
Modified residue10411Phosphoserine Ref.20
Modified residue11761Phosphotyrosine Ref.20
Modified residue12171Phosphoserine Ref.16 Ref.22 Ref.24
Modified residue15191N6-acetyllysine Ref.21
Modified residue16471Phosphoserine Ref.22
Modified residue20521N6-acetyllysine Ref.21
Modified residue24211N6-acetyllysine Ref.21

Natural variations

Alternative sequence1053 – 107220Missing in isoform 3.
VSP_012271
Alternative sequence15861Q → QLSKLL in isoform 2.
VSP_012270
Natural variant3851N → S.
Corresponds to variant rs2227863 [ dbSNP | Ensembl ].
VAR_038513
Natural variant9041S → C in a breast cancer sample; somatic mutation. Ref.27
VAR_035454
Natural variant10171P → S in a breast cancer sample; somatic mutation. Ref.27
VAR_035455
Natural variant13001I → T. Ref.1 Ref.8 Ref.9
Corresponds to variant rs1048236 [ dbSNP | Ensembl ].
VAR_012227
Natural variant17941R → W in a breast cancer sample; somatic mutation. Ref.27
VAR_035456
Natural variant19181D → N in a breast cancer sample; somatic mutation. Ref.27
VAR_035457
Natural variant22021Missing in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. Ref.28
VAR_063886
Natural variant23031R → RM in EIEE5; could form a heterodimer with SPTBN1 but the heterodimer is thermally unstable; suggests a dominant negative effect. Ref.28
VAR_063887

Experimental info

Sequence conflict1501K → N in AAA51790. Ref.1
Sequence conflict4981S → F in AAA51790. Ref.1
Sequence conflict7371I → V in AAA51790. Ref.1
Sequence conflict7371I → V in AAA52468. Ref.8
Sequence conflict7371I → V in AAA51702. Ref.9
Sequence conflict15951F → R in AAA52468. Ref.8
Sequence conflict15951F → R in AAA51702. Ref.9
Sequence conflict16251S → N in AAA51790. Ref.1
Sequence conflict1670 – 16712FD → IA in AAA51790. Ref.1
Sequence conflict19181D → A in AAA51790. Ref.1
Sequence conflict1971 – 19722KL → NV in AAA51790. Ref.1
Sequence conflict1971 – 19722KL → NV in AAB41498. Ref.2
Sequence conflict21631A → R in CAA60503. Ref.13
Sequence conflict2347 – 23482EF → DG in AAA51790. Ref.1
Sequence conflict24481Y → I in AAA51790. Ref.1

Secondary structure

............................ 2472
Helix Strand Turn

Details...

Sequences

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

Last modified May 2, 2006. Version 3.
Checksum: 4433BF74EFCEFC8A

FASTA2,472284,539
        10         20         30         40         50         60 
MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI 

        70         80         90        100        110        120 
QEKLQIASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI 

       130        140        150        160        170        180 
RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD 

       190        200        210        220        230        240 
LEHVEVLQKK FEEFQTDMAA HEERVNEVNQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL 

       250        260        270        280        290        300 
KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QALLRKHEGL 

       310        320        330        340        350        360 
ERDLAALEDK VKALCAEADR LQQSHPLSAT QIQVKREELI TNWEQIRTLA AERHARLNDS 

       370        380        390        400        410        420 
YRLQRFLADF RDLTSWVTEM KALINADELA SDVAGAEALL DRHQEHKGEI DAHEDSFKSA 

       430        440        450        460        470        480 
DESGQALLAA GHYASDEVRE KLTVLSEERA ALLELWELRR QQYEQCMDLQ LFYRDTEQVD 

       490        500        510        520        530        540 
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA 

       550        560        570        580        590        600 
MEDVATRRDA LLSRRNALHE RAMRRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA 

       610        620        630        640        650        660 
YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKDEVA ARMNEVISLW 

       670        680        690        700        710        720 
KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH 

       730        740        750        760        770        780 
ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL 

       790        800        810        820        830        840 
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI 

       850        860        870        880        890        900 
KAVTQKGNAM VEEGHFAAED VKAKLHELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN 

       910        920        930        940        950        960 
EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV 

       970        980        990       1000       1010       1020 
APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY 

      1030       1040       1050       1060       1070       1080 
VKKLDPAQSA SRENLLEEQG SIALRQEQID NQTRITKEAG SVSLRMKQVE ELYHSLLELG 

      1090       1100       1110       1120       1130       1140 
EKRKGMLEKS CKKFMLFREA NELQQWINEK EAALTSEEVG ADLEQVEVLQ KKFDDFQKDL 

      1150       1160       1170       1180       1190       1200 
KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGMMP RDETDSKTAS PWKSARLMVH 

      1210       1220       1230       1240       1250       1260 
TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN 

      1270       1280       1290       1300       1310       1320 
YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAERLI QSHPESAEDL QEKCTELNQA 

      1330       1340       1350       1360       1370       1380 
WSSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER 

      1390       1400       1410       1420       1430       1440 
HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKQKL DILDQERADL EKAWVQRRMM 

      1450       1460       1470       1480       1490       1500 
LDQCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK 

      1510       1520       1530       1540       1550       1560 
IAALQAFADQ LIAAGHYAKG DISSRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV 

      1570       1580       1590       1600       1610       1620 
DEIEAWISEK LQTASDESYK DPTNIQSKHQ KHQAFEAELH ANADRIRGVI DMGNSLIERG 

      1630       1640       1650       1660       1670       1680 
ACAGSEDAVK ARLAALADQW QFLVQKSAEK SQKLKEANKQ QNFNTGIKDF DFWLSEVEAL 

      1690       1700       1710       1720       1730       1740 
LASEDYGKDL ASVNNLLKKH QLLEADISAH EDRLKDLNSQ ADSLMTSSAF DTSQVKDKRD 

      1750       1760       1770       1780       1790       1800 
TINGRFQKIK SMAASRRAKL NESHRLHQFF RDMDDEESWI KEKKLLVGSE DYGRDLTGVQ 

      1810       1820       1830       1840       1850       1860 
NLRKKHKRLE AELAAHEPAI QGVLDTGKKL SDDNTIGKEE IQQRLAQFVE HWKELKQLAA 

      1870       1880       1890       1900       1910       1920 
ARGQRLEESL EYQQFVANVE EEEAWINEKM TLVASEDYGD TLAAIQGLLK KHEAFETDFT 

      1930       1940       1950       1960       1970       1980 
VHKDRVNDVC TNGQDLIKKN NHHEENISSK MKGLNGKVSD LEKAAAQRKA KLDENSAFLQ 

      1990       2000       2010       2020       2030       2040 
FNWKADVVES WIGEKENSLK TDDYGRDLSS VQTLLTKQET FDAGLQAFQQ EGIANITALK 

      2050       2060       2070       2080       2090       2100 
DQLLAAKHVQ SKAIEARHAS LMKRWSQLLA NSAARKKKLL EAQSHFRKVE DLFLTFAKKA 

      2110       2120       2130       2140       2150       2160 
SAFNSWFENA EEDLTDPVRC NSLEEIKALR EAHDAFRSSL SSAQADFNQL AELDRQIKSF 

      2170       2180       2190       2200       2210       2220 
RVASNPYTWF TMEALEETWR NLQKIIKERE LELQKEQRRQ EENDKLRQEF AQHANAFHQW 

      2230       2240       2250       2260       2270       2280 
IQETRTYLLD GSCMVEESGT LESQLEATKR KHQEIRAMRS QLKKIEDLGA AMEEALILDN 

      2290       2300       2310       2320       2330       2340 
KYTEHSTVGL AQQWDQLDQL GMRMQHNLEQ QIQARNTTGV TEEALKEFSM MFKHFDKDKS 

      2350       2360       2370       2380       2390       2400 
GRLNHQEFKS CLRSLGYDLP MVEEGEPDPE FEAILDTVDP NRDGHVSLQE YMAFMISRET 

      2410       2420       2430       2440       2450       2460 
ENVKSSEEIE SAFRALSSEG KPYVTKEELY QNLTREQADY CVSHMKPYVD GKGRELPTAF 

      2470 
DYVEFTRSLF VN 

« Hide

Isoform 2 [UniParc].

Checksum: 66DC2E2F50E89E1E
Show »

FASTA2,477285,094
Isoform 3 [UniParc].

Checksum: A34BBE6ADCAF5A5C
Show »

FASTA2,452282,282

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Erratum
McMahon A.P., Giebelhaus D.H., Champion J.E., Bailes J.A., Lacey S., Carritt B., Henchman S.K., Moon R.T.
Differentiation 34:241-241(1987)
[11]"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.
[12]"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.
[13]"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.
[14]"Tyrosine phosphorylation regulates alpha II spectrin cleavage by calpain."
Nicolas G., Fournier C.M., Galand C., Malbert-Colas L., Bournier O., Kroviarski Y., Bourgeois M., Camonis J.H., Dhermy D., Grandchamp B., Lecomte M.-C.
Mol. Cell. Biol. 22:3527-3536(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACP1.
[15]"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.
[16]"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.
[17]"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.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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.
[21]"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].
[22]"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.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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].
[25]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"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.
[27]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-904; SER-1017; TRP-1794 AND ASN-1918.
[28]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA35715.
RefSeqNP_001123910.1. NM_001130438.2.
NP_001182461.1. NM_001195532.1.
NP_003118.2. NM_003127.3.
UniGeneHs.372331.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FOTX-ray2.45C1172-1210[»]
3F31X-ray2.30A/B1-147[»]
3FB2X-ray2.30A/B1337-1544[»]
ProteinModelPortalQ13813.
SMRQ13813. Positions 8-2470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112587. 109 interactions.
DIPDIP-33141N.
IntActQ13813. 45 interactions.
MINTMINT-4999298.

PTM databases

PhosphoSiteQ13813.

Polymorphism databases

DMDM94730425.

Proteomic databases

PaxDbQ13813.
PRIDEQ13813.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372731; ENSP00000361816; ENSG00000197694. [Q13813-1]
ENST00000372739; ENSP00000361824; ENSG00000197694. [Q13813-2]
GeneID6709.
KEGGhsa:6709.
UCSCuc004bvl.4. human. [Q13813-1]
uc004bvm.4. human. [Q13813-2]
uc004bvn.4. human. [Q13813-3]

Organism-specific databases

CTD6709.
GeneCardsGC09P131314.
HGNCHGNC:11273. SPTAN1.
HPACAB004581.
HPA007927.
MIM182810. gene.
613477. phenotype.
neXtProtNX_Q13813.
Orphanet1934. Early infantile epileptic encephalopathy.
PharmGKBPA36102.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOVERGENHBG059266.
KOK06114.
OrthoDBEOG7GXP9K.
PhylomeDBQ13813.
TreeFamTF343803.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_188576. Developmental Biology.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ13813.
BgeeQ13813.
GenevestigatorQ13813.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. 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]
PfamPF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTSM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPTAN1. human.
EvolutionaryTraceQ13813.
GeneWikiSPTAN1.
GenomeRNAi6709.
NextBio26162.
PROQ13813.
SOURCESearch...

Entry information

Entry nameSPTN1_HUMAN
AccessionPrimary (citable) accession number: Q13813
Secondary accession number(s): Q13186 expand/collapse secondary AC list , Q15324, Q16606, Q59EF1, Q5VXV5, Q5VXV6, Q7Z6M5, Q9P0V0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM