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P02549 (SPTA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 177. 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, erythrocytic 1
Alternative name(s):
Erythroid alpha-spectrin
Gene names
Name:SPTA1
Synonyms:SPTA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.12 Ref.14

Subcellular location

Cytoplasmcytoskeleton. Cytoplasmcell cortex.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28

Hereditary pyropoikilocytosis (HPP) [MIM:266140]: Autosomal recessive hematologic disorder characterized by hemolytic anemia, microspherocytosis, poikilocytosis, and an unusual thermal sensitivity of red cells.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

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.

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.

Sequence similarities

Belongs to the spectrin family.

Contains 3 EF-hand domains.

Contains 1 SH3 domain.

Contains 21 spectrin repeats.

Ontologies

Keywords
   Biological processCell shape
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Elliptocytosis
Hereditary hemolytic anemia
Pyropoikilocytosis
   DomainRepeat
SH3 domain
   LigandActin-binding
Calcium
Metal-binding
   Molecular functionActin capping
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

actin filament organization

Traceable author statement Ref.9. Source: ProtInc

axon guidance

Traceable author statement. Source: Reactome

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

lymphocyte homeostasis

Inferred from electronic annotation. Source: Ensembl

plasma membrane organization

Inferred from electronic annotation. Source: Ensembl

porphyrin-containing compound biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentactin cytoskeleton

Traceable author statement PubMed 10950304. Source: BHF-UCL

cuticular plate

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

intrinsic component of the cytoplasmic side of the plasma membrane

Traceable author statement PubMed 10950304. Source: BHF-UCL

spectrin

Traceable author statement Ref.9. Source: ProtInc

spectrin-associated cytoskeleton

Inferred from direct assay PubMed 379653. Source: BHF-UCL

   Molecular_functionactin filament binding

Traceable author statement Ref.9. Source: ProtInc

calcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 12820899PubMed 9593709. Source: IntAct

structural constituent of cytoskeleton

Traceable author statement Ref.9. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABI1Q8IZP02EBI-375617,EBI-375446
SPTBN1Q010823EBI-375617,EBI-351561

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P02549-1)

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: P02549-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1889-1891: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24192419Spectrin alpha chain, erythrocytic 1
PRO_0000073452

Regions

Repeat19 – 5133Spectrin 1
Repeat53 – 156104Spectrin 2
Repeat158 – 262105Spectrin 3
Repeat264 – 368105Spectrin 4
Repeat370 – 474105Spectrin 5
Repeat476 – 580105Spectrin 6
Repeat582 – 685104Spectrin 7
Repeat687 – 791105Spectrin 8
Repeat793 – 897105Spectrin 9
Repeat899 – 96870Spectrin 10
Domain977 – 103660SH3
Repeat1082 – 1181100Spectrin 11
Repeat1183 – 1287105Spectrin 12
Repeat1289 – 1393105Spectrin 13
Repeat1395 – 1498104Spectrin 14
Repeat1500 – 1605106Spectrin 15
Repeat1607 – 1711105Spectrin 16
Repeat1713 – 1817105Spectrin 17
Repeat1819 – 1926108Spectrin 18
Repeat1928 – 2033106Spectrin 19
Repeat2043 – 2147105Spectrin 20
Repeat2157 – 2258102Spectrin 21
Domain2271 – 230636EF-hand 1
Domain2314 – 234936EF-hand 2
Domain2352 – 238635EF-hand 3
Calcium binding2284 – 2295121 Potential
Calcium binding2327 – 2338122 Potential

Natural variations

Alternative sequence1889 – 18913Missing in isoform 2.
VSP_037662
Natural variant241I → S in EL2; Lograno. Ref.16
VAR_001324
Natural variant281R → C in EL2. Ref.17
VAR_001328
Natural variant281R → H in EL2; Corbeil. Ref.17
Corresponds to variant rs28934004 [ dbSNP | Ensembl ].
VAR_001325
Natural variant281R → L in EL2. Ref.17
VAR_001326
Natural variant281R → S in EL2. Ref.17 Ref.18
Corresponds to variant rs28934005 [ dbSNP | Ensembl ].
VAR_001327
Natural variant311V → A in EL2; Marseille.
VAR_001329
Natural variant341R → W in EL2; Genova. Ref.27
VAR_001330
Natural variant411R → W in EL2; Tunis. Ref.26
VAR_001331
Natural variant451R → S in EL2; Clichy. Ref.19
VAR_001332
Natural variant451R → T in EL2; Anastasia. Ref.28
VAR_001333
Natural variant461G → V in EL2; Culoz. Ref.24
VAR_001334
Natural variant481K → R in HPP. Ref.18
VAR_001335
Natural variant491L → F in EL2; Lyon. Ref.24
VAR_001336
Natural variant1091S → F.
Corresponds to variant rs3737521 [ dbSNP | Ensembl ].
VAR_038506
Natural variant1511G → D in EL2; Ponte de Sor.
VAR_001337
Natural variant1521D → N.
Corresponds to variant rs16840544 [ dbSNP | Ensembl ].
VAR_038507
Natural variant1541L → LL in EL2.
VAR_001338
Natural variant2071L → P in EL2 and HPP; Saint-Louis. Ref.20
Corresponds to variant rs121918643 [ dbSNP | Ensembl ].
VAR_001339
Natural variant2601L → P in EL2; Nigerian. Ref.3
VAR_001340
Natural variant2611S → P in EL2. Ref.3
VAR_001341
Natural variant4691H → P in EL2; Barcelona. Ref.22
VAR_001342
Natural variant4691Missing in EL2; Alexandria.
VAR_001343
Natural variant4711Q → P in EL2. Ref.3
VAR_001344
Natural variant7011R → H.
Corresponds to variant rs12090314 [ dbSNP | Ensembl ].
VAR_001345
Natural variant7661A → T.
Corresponds to variant rs11265047 [ dbSNP | Ensembl ].
VAR_038508
Natural variant7911D → E in EL2; Jendouba. Ref.25
Corresponds to variant rs7418956 [ dbSNP | Ensembl ].
VAR_001346
Natural variant8091I → V.
Corresponds to variant rs7547313 [ dbSNP | Ensembl ].
VAR_001347
Natural variant8531T → R.
Corresponds to variant rs35121052 [ dbSNP | Ensembl ].
VAR_001348
Natural variant9571A → V.
Corresponds to variant rs34706737 [ dbSNP | Ensembl ].
VAR_038509
Natural variant9701A → D.
Corresponds to variant rs35948326 [ dbSNP | Ensembl ].
VAR_001349
Natural variant11631S → A. Ref.1
Corresponds to variant rs2482965 [ dbSNP | Ensembl ].
VAR_038510
Natural variant13301R → I.
Corresponds to variant rs34214405 [ dbSNP | Ensembl ].
VAR_038511
Natural variant15681C → R. Ref.1 Ref.7
Corresponds to variant rs863931 [ dbSNP | Ensembl ].
VAR_038512
Natural variant16931K → Q.
Corresponds to variant rs857725 [ dbSNP | Ensembl ].
VAR_059199
Natural variant18361N → S.
Corresponds to variant rs16830483 [ dbSNP | Ensembl ].
VAR_059200
Natural variant18581L → V. Ref.21
Corresponds to variant rs3737515 [ dbSNP | Ensembl ].
VAR_001350
Natural variant20251A → G in Cagliari. Ref.23
VAR_001351
Natural variant22651I → T.
Corresponds to variant rs952094 [ dbSNP | Ensembl ].
VAR_059201

Experimental info

Sequence conflict119 – 13012Missing in AAA60575. Ref.3
Sequence conflict3951A → G in AAA60575. Ref.3
Sequence conflict14101W → R in AAA60577. Ref.1
Sequence conflict14101W → R in AAA60994. Ref.1
Sequence conflict15701Missing in AAA60577. Ref.1
Sequence conflict15701Missing in AAA60994. Ref.1
Sequence conflict15701Missing in AAA60569. Ref.7
Sequence conflict18911Q → H in AAA60577. Ref.1
Sequence conflict18911Q → H in AAA60994. Ref.1
Sequence conflict2400 – 241920GRSHL…SYFGN → VEAISLAMTTLASPIPTLAT NKQLLVDRRKS in AAA60577. Ref.1
Sequence conflict2400 – 241920GRSHL…SYFGN → VEAISLAMTTLASPIPTLAT NKQLLVDRRKS in AAA60994. Ref.1

Secondary structure

............ 2419
Helix Strand Turn

Details...

Sequences

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

Last modified October 5, 2010. Version 5.
Checksum: B60680145C58DF55

FASTA2,419280,014
        10         20         30         40         50         60 
MEQFPKETVV ESSGPKVLET AEEIQERRQE VLTRYQSFKE RVAERGQKLE DSYHLQVFKR 

        70         80         90        100        110        120 
DADDLGKWIM EKVNILTDKS YEDPTNIQGK YQKHQSLEAE VQTKSRLMSE LEKTREERFT 

       130        140        150        160        170        180 
MGHSAHEETK AHIEELRHLW DLLLELTLEK GDQLLRALKF QQYVQECADI LEWIGDKEAI 

       190        200        210        220        230        240 
ATSVELGEDW ERTEVLHKKF EDFQVELVAK EGRVVEVNQY ANECAEENHP DLPLIQSKQN 

       250        260        270        280        290        300 
EVNAAWERLR GLALQRQKAL SNAANLQRFK RDVTEAIQWI KEKEPVLTSE DYGKDLVASE 

       310        320        330        340        350        360 
GLFHSHKGLE RNLAVMSDKV KELCAKAEKL TLSHPSDAPQ IQEMKEDLVS SWEHIRALAT 

       370        380        390        400        410        420 
SRYEKLQATY WYHRFSSDFD ELSGWMNEKT AAINADELPT DVAGGEVLLD RHQQHKHEID 

       430        440        450        460        470        480 
SYDDRFQSAD ETGQDLVNAN HEASDEVREK MEILDNNWTA LLELWDERHR QYEQCLDFHL 

       490        500        510        520        530        540 
FYRDSEQVDS WMSRQEAFLE NEDLGNSLGS AEALLQKHED FEEAFTAQEE KIITVDKTAT 

       550        560        570        580        590        600 
KLIGDDHYDS ENIKAIRDGL LARRDALREK AATRRRLLKE SLLLQKLYED SDDLKNWINK 

       610        620        630        640        650        660 
KKKLADDEDY KDIQNLKSRV QKQQVFEKEL AVNKTQLENI QKTGQEMIEG GHYASDNVTT 

       670        680        690        700        710        720 
RLSEVASLWE ELLEATKQKG TQLHEANQQL QFENNAEDLQ RWLEDVEWQV TSEDYGKGLA 

       730        740        750        760        770        780 
EVQNRLRKHG LLESAVAARQ DQVDILTDLA AYFEEIGHPD SKDIRARQES LVCRFEALKE 

       790        800        810        820        830        840 
PLATRKKKLL DLLHLQLICR DTEDEEAWIQ ETEPSATSTY LGKDLIASKK LLNRHRVILE 

       850        860        870        880        890        900 
NIASHEPRIQ EITERGNKMV EEGHFAAEDV ASRVKSLNQN MESLRARAAR RQNDLEANVQ 

       910        920        930        940        950        960 
FQQYLADLHE AETWIREKEP IVDNTNYGAD EEAAGALLKK HEAFLLDLNS FGDSMKALRN 

       970        980        990       1000       1010       1020 
QANACQQQQA APVEGVAGEQ RVMALYDFQA RSPREVTMKK GDVLTLLSSI NKDWWKVEAA 

      1030       1040       1050       1060       1070       1080 
DHQGIVPAVY VRRLAHDEFP MLPQRRREEP GNITQRQEQI ENQYRSLLDR AEERRRRLLQ 

      1090       1100       1110       1120       1130       1140 
RYNEFLLAYE AGDMLEWIQE KKAENTGVEL DDVWELQKKF DEFQKDLNTN EPRLRDINKV 

      1150       1160       1170       1180       1190       1200 
ADDLLFEGLL TPEGAQIRQE LNSRWGSLQR LADEQRQLLG SAHAVEVFHR EADDTKEQIE 

      1210       1220       1230       1240       1250       1260 
KKCQALSAAD PGSDLFSVQA LQRRHEGFER DLVPLGDKVT ILGETAERLS ESHPDATEDL 

      1270       1280       1290       1300       1310       1320 
QRQKMELNEA WEDLQGRTKD RKESLNEAQK FYLFLSKARD LQNWISSIGG MVSSQELAED 

      1330       1340       1350       1360       1370       1380 
LTGIEILLER HQEHRADMEA EAPTFQALED FSAELIDSGH HASPEIEKKL QAVKLERDDL 

      1390       1400       1410       1420       1430       1440 
EKAWEKRKKI LDQCLELQMF QGNCDQVESW MVARENSLRS DDKSSLDSLE ALMKKRDDLD 

      1450       1460       1470       1480       1490       1500 
KAITAQEGKI TDLEHFAESL IADEHYAKEE IATRLQRVLD RWKALKAQLI DERTKLGDYA 

      1510       1520       1530       1540       1550       1560 
NLKQFYRDLE ELEEWISEML PTACDESYKD ATNIQRKYLK HQTFAHEVDG RSEQVHGVIN 

      1570       1580       1590       1600       1610       1620 
LGNSLIECSA CDGNEEAMKE QLEQLKEHWD HLLERTNDKG KKLNEASRQQ RFNTSIRDFE 

      1630       1640       1650       1660       1670       1680 
FWLSEAETLL AMKDQARDLA SAGNLLKKHQ LLEREMLARE DALKDLNTLA EDLLSSGTFN 

      1690       1700       1710       1720       1730       1740 
VDQIVKKKDN VNKRFLNVQE LAAAHHEKLK EAYALFQFFQ DLDDEESWIE EKLIRVSSQD 

      1750       1760       1770       1780       1790       1800 
YGRDLQGVQN LLKKHKRLEG ELVAHEPAIQ NVLDMAEKLK DKAAVGQEEI QLRLAQFVEH 

      1810       1820       1830       1840       1850       1860 
WEKLKELAKA RGLKLEESLE YLQFMQNAEE EEAWINEKNA LAVRGDCGDT LAATQSLLMK 

      1870       1880       1890       1900       1910       1920 
HEALENDFAV HETRVQNVCA QGEDILNKVL QEESQNKEIS SKIEALNEKT PSLAKAIAAW 

      1930       1940       1950       1960       1970       1980 
KLQLEDDYAF QEFNWKADVV EAWIADKETS LKTNGNGADL GDFLTLLAKQ DTLDASLQSF 

      1990       2000       2010       2020       2030       2040 
QQERLPEITD LKDKLISAQH NQSKAIEERY AALLKRWEQL LEASAVHRQK LLEKQLPLQK 

      2050       2060       2070       2080       2090       2100 
AEDLFVEFAH KASALNNWCE KMEENLSEPV HCVSLNEIRQ LQKDHEDFLA SLARAQADFK 

      2110       2120       2130       2140       2150       2160 
CLLELDQQIK ALGVPSSPYT WLTVEVLERT WKHLSDIIEE REQELQKEEA RQVKNFEMCQ 

      2170       2180       2190       2200       2210       2220 
EFEQNASTFL QWILETRAYF LDGSLLKETG TLESQLEANK RKQKEIQAMK RQLTKIVDLG 

      2230       2240       2250       2260       2270       2280 
DNLEDALILD IKYSTIGLAQ QWDQLYQLGL RMQHNLEQQI QAKDIKGVSE ETLKEFSTIY 

      2290       2300       2310       2320       2330       2340 
KHFDENLTGR LTHKEFRSCL RGLNYYLPMV EEDEHEPKFE KFLDAVDPGR KGYVSLEDYT 

      2350       2360       2370       2380       2390       2400 
AFLIDKESEN IKSSDEIENA FQALAEGKSY ITKEDMKQAL TPEQVSFCAT HMQQYMDPRG 

      2410 
RSHLSGYDYV GFTNSYFGN 

« Hide

Isoform 2 [UniParc].

Checksum: C3824332610EF99C
Show »

FASTA2,416279,674

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61826 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
CCDSCCDS41423.1. [P02549-1]
PIRSJHUA. A35716.
RefSeqNP_003117.2. NM_003126.2. [P02549-1]
UniGeneHs.119825.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OWANMR-A1-156[»]
3LBXX-ray2.80A1-158[»]
ProteinModelPortalP02549.
SMRP02549. Positions 1-953, 993-1034, 1049-2264, 2267-2415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112586. 19 interactions.
DIPDIP-1020N.
DIP-17031N.
IntActP02549. 12 interactions.
MINTMINT-7211599.
STRING9606.ENSP00000357130.

PTM databases

PhosphoSiteP02549.

Polymorphism databases

DMDM308153675.

Proteomic databases

MaxQBP02549.
PaxDbP02549.
PRIDEP02549.

Protocols and materials databases

DNASU6708.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368147; ENSP00000357129; ENSG00000163554. [P02549-1]
GeneID6708.
KEGGhsa:6708.
UCSCuc001fst.1. human. [P02549-1]

Organism-specific databases

CTD6708.
GeneCardsGC01M158580.
H-InvDBHIX0028529.
HGNCHGNC:11272. SPTA1.
HPACAB016193.
CAB037246.
HPA028048.
HPA028253.
MIM130600. phenotype.
182860. gene.
266140. phenotype.
270970. phenotype.
neXtProtNX_P02549.
Orphanet98864. Common hereditary elliptocytosis.
98867. Hereditary pyropoikilocytosis.
822. Hereditary spherocytosis.
PharmGKBPA36101.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237318.
HOGENOMHOG000246965.
HOVERGENHBG059266.
InParanoidP02549.
KOK06114.
OMASINKDWW.
OrthoDBEOG7GXP9K.
PhylomeDBP02549.
TreeFamTF343803.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressP02549.
BgeeP02549.
CleanExHS_SPTA1.
GenevestigatorP02549.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. 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]
PfamPF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSPR01887. SPECTRNALPHA.
SMARTSM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPTA1. human.
EvolutionaryTraceP02549.
GeneWikiSpectrin,_alpha_1.
GenomeRNAi6708.
NextBio26158.
PROP02549.
SOURCESearch...

Entry information

Entry nameSPTA1_HUMAN
AccessionPrimary (citable) accession number: P02549
Secondary accession number(s): Q15514 expand/collapse secondary AC list , Q5VYL1, Q5VYL2, Q6LDY5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 177 of the entry and version 5 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 1

Human chromosome 1: entries, gene names and cross-references to MIM