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P02549

- SPTA1_HUMAN

UniProt

P02549 - SPTA1_HUMAN

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Protein

Spectrin alpha chain, erythrocytic 1

Gene
SPTA1, SPTA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi2284 – 2295121 Reviewed predictionAdd
BLAST
Calcium bindingi2327 – 2338122 Reviewed predictionAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Cell shape

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:11272. SPTA1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Disease mutation, Elliptocytosis, Hereditary hemolytic anemia, Pyropoikilocytosis

Organism-specific databases

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

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiP02549.
PaxDbiP02549.
PRIDEiP02549.

PTM databases

PhosphoSiteiP02549.

Expressioni

Gene expression databases

ArrayExpressiP02549.
BgeeiP02549.
CleanExiHS_SPTA1.
GenevestigatoriP02549.

Organism-specific databases

HPAiCAB016193.
CAB037246.
HPA028048.
HPA028253.

Interactioni

Subunit structurei

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

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP02549.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati19 – 5133Spectrin 1Add
BLAST
Repeati53 – 156104Spectrin 2Add
BLAST
Repeati158 – 262105Spectrin 3Add
BLAST
Repeati264 – 368105Spectrin 4Add
BLAST
Repeati370 – 474105Spectrin 5Add
BLAST
Repeati476 – 580105Spectrin 6Add
BLAST
Repeati582 – 685104Spectrin 7Add
BLAST
Repeati687 – 791105Spectrin 8Add
BLAST
Repeati793 – 897105Spectrin 9Add
BLAST
Repeati899 – 96870Spectrin 10Add
BLAST
Domaini977 – 103660SH3Add
BLAST
Repeati1082 – 1181100Spectrin 11Add
BLAST
Repeati1183 – 1287105Spectrin 12Add
BLAST
Repeati1289 – 1393105Spectrin 13Add
BLAST
Repeati1395 – 1498104Spectrin 14Add
BLAST
Repeati1500 – 1605106Spectrin 15Add
BLAST
Repeati1607 – 1711105Spectrin 16Add
BLAST
Repeati1713 – 1817105Spectrin 17Add
BLAST
Repeati1819 – 1926108Spectrin 18Add
BLAST
Repeati1928 – 2033106Spectrin 19Add
BLAST
Repeati2043 – 2147105Spectrin 20Add
BLAST
Repeati2157 – 2258102Spectrin 21Add
BLAST
Domaini2271 – 230636EF-hand 1Add
BLAST
Domaini2314 – 234936EF-hand 2Add
BLAST
Domaini2352 – 238635EF-hand 3Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

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

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P02549-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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

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

Note: Gene prediction based on EST data.

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

Natural variant

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1889 – 18913Missing in isoform 2. VSP_037662

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 13012Missing in AAA60575. 1 PublicationAdd
BLAST
Sequence conflicti395 – 3951A → G in AAA60575. 1 Publication
Sequence conflicti1410 – 14101W → R in AAA60577. 1 Publication
Sequence conflicti1410 – 14101W → R in AAA60994. 1 Publication
Sequence conflicti1570 – 15701Missing in AAA60577. 1 Publication
Sequence conflicti1570 – 15701Missing in AAA60994. 1 Publication
Sequence conflicti1570 – 15701Missing in AAA60569. 1 Publication
Sequence conflicti1891 – 18911Q → H in AAA60577. 1 Publication
Sequence conflicti1891 – 18911Q → H in AAA60994. 1 Publication
Sequence conflicti2400 – 241920GRSHL…SYFGN → VEAISLAMTTLASPIPTLAT NKQLLVDRRKS in AAA60577. 1 PublicationAdd
BLAST
Sequence conflicti2400 – 241920GRSHL…SYFGN → VEAISLAMTTLASPIPTLAT NKQLLVDRRKS in AAA60994. 1 PublicationAdd
BLAST

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi308153675.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSitei P02549.

Polymorphism databases

DMDMi 308153675.

Proteomic databases

MaxQBi P02549.
PaxDbi P02549.
PRIDEi P02549.

Protocols and materials databases

DNASUi 6708.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

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

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin."
    Sahr K.E., Laurila P., Kotula L., Scarpa A.L., Coupal E., Leto T.L., Linnenbach A.J., Winkelmann J.C., Speicher D.W., Marchesi V.T., Curtis P.J., Forget B.G.
    J. Biol. Chem. 265:4434-4443(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS ALA-1163 AND ARG-1568.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Sequence and exon-intron organization of the DNA encoding the alpha I domain of human spectrin. Application to the study of mutations causing hereditary elliptocytosis."
    Sahr K.E., Tobe T., Scarpa A., Laughinghouse K., Marchesi S.L., Agre P., Linnenbach A.J., Marchesi V.T., Forget B.G.
    J. Clin. Invest. 84:1243-1252(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-533, VARIANTS EL2 PRO-260; PRO-261 AND PRO-471.
  4. "Structure of human erythrocyte spectrin. II. The sequence of the alpha-I domain."
    Speicher D.W., Davis G., Marchesi V.T.
    J. Biol. Chem. 258:14938-14947(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-601.
  5. "Structure of human erythrocyte spectrin. I. Isolation of the alpha-I domain and its cyanogen bromide peptides."
    Speicher D.W., Davis G., Yurchenco P.D., Marchesi V.T.
    J. Biol. Chem. 258:14931-14937(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-125.
  6. "Cloning of a portion of the chromosomal gene for human erythrocyte alpha-spectrin by using a synthetic gene fragment."
    Linnenbach A.J., Speicher D.W., Marchesi V.T., Forget B.G.
    Proc. Natl. Acad. Sci. U.S.A. 83:2397-2401(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 320-450.
  7. "Sequence comparison of human and murine erythrocyte alpha-spectrin cDNA."
    Curtis P.J., Palumbo A., Ming J., Fraser P.J., Cioe L., Meo P., Shane S., Rovera G.
    Gene 36:357-362(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1451-1688, VARIANT ARG-1568.
  8. "Erythrocyte spectrin is comprised of many homologous triple helical segments."
    Speicher D.W., Marchesi V.T.
    Nature 311:177-180(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  9. "Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site."
    Speicher D.W., Weglarz L., DeSilva T.M.
    J. Biol. Chem. 267:14775-14782(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-16; 46-55; 680-689; 1047-1056 AND 1922-1931.
  10. "The first human alpha-spectrin structural domain begins with serine."
    Lusitani D.M., Qtaishat N., LaBrake C.C., Yu R.N., Davis J., Kelley M.R., Fung L.W.-M.
    J. Biol. Chem. 269:25955-25958(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-28; 39-44 AND 50-59.
  11. Gibson T.J.
    Unpublished observations (MAR-1995)
    Cited for: IDENTIFICATION OF PROBABLE FRAMESHIFT IN 2408-2419.
  12. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
    Voss M., Lettau M., Janssen O.
    BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FASLG.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structural studies on human erythrocyte alpha-spectrin tetramerization site."
    Park S., Caffrey M.S., Johnson M.E., Fung L.W.-M.
    J. Biol. Chem. 278:21837-21844(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-156, SUBUNIT.
  15. "Spectrin mutations in hereditary elliptocytosis and hereditary spherocytosis."
    Maillet P., Alloisio N., Morle L., Delaunay J.
    Hum. Mutat. 8:97-107(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  16. "Identification of three novel spectrin alpha I/74 mutations in hereditary elliptocytosis: further support for a triple-stranded folding unit model of the spectrin heterodimer contact site."
    Parquet N., Devaux I., Boulanger L., Galand C., Boivin P., Lecomte M.-C., Dhermy D., Garbarz M.
    Blood 84:303-308(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 SER-24.
  17. "Four different mutations in codon 28 of alpha spectrin are associated with structurally and functionally abnormal spectrin alpha I/74 in hereditary elliptocytosis."
    Coetzer T.L., Sahr K., Prchal J., Blacklock H., Peterson L., Koler R., Doyle J., Manaster J., Palek J.
    J. Clin. Invest. 88:743-749(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EL2 CYS-28; HIS-28; LEU-28 AND SER-28.
  18. "Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha I/74-kilodalton tryptic peptide."
    Floyd P.B., Gallagher P.G., Valentino L.A., Davis M., Marchesi S.L., Forget B.G.
    Blood 78:1364-1372(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 SER-28, VARIANT HPP ARG-48.
  19. "Sp alpha I/78: a mutation of the alpha I spectrin domain in a white kindred with HE and HPP phenotypes."
    Lecomte M.-C., Garbarz M., Grandchamp B., Feo C., Gautero H., Devaux I., Bournier O., Galand C., D'Auriol L., Galibert F., Sahr K.E., Forget B.G., Boivin P., Dhermy D.
    Blood 74:1126-1133(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 SER-45.
  20. "A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin."
    Gallagher P.G., Tse W.T., Coetzer T., Lecomte M.-C., Garbarz M., Zarkowsky H.S., Baruchel A., Ballas S.K., Dhermy D., Palek J., Forget B.G.
    J. Clin. Invest. 89:892-898(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2/HPP PRO-207.
  21. "Low expression allele alpha LELY of red cell spectrin is associated with mutations in exon 40 (alpha V/41 polymorphism) and intron 45 and with partial skipping of exon 46."
    Wilmotte R., Marechal J., Morle L., Baklouti F., Philippe N., Kastally R., Kotula L., Delaunay J., Alloisio N.
    J. Clin. Invest. 91:2091-2096(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VAL-1858.
  22. "Elliptopoikilocytosis associated with the alpha 469 His-->Pro mutation in spectrin Barcelona (alpha I/50-46b)."
    dalla Venezia N., Alloisio N., Forissier A., Denoroy L., Aymerich M., Vives-Corrons J.L., Besalduch J., Besson I., Delaunay J.
    Blood 82:1661-1665(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 BARCELONA PRO-469.
  23. "Spectrin Cagliari: an Ala-->Gly substitution in helix 1 of beta spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer."
    Sahr K.E., Coetzer T.L., Moy L.S., Derick L.H., Chishti A.H., Jarolim P., Lorenzo F., del Giudice E.M., Iolascon A., Gallanello R., Cao A., Delaunay J., Liu S.-C., Palek J.
    J. Biol. Chem. 268:22656-22662(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CAGLIARI GLY-2025.
  24. "Two elliptocytogenic alpha I/74 variants of the spectrin alpha I domain. Spectrin Culoz (GGT-->GTT; alpha I 40 Gly-->Val) and spectrin Lyon (CTT-->TTT; alpha I 43 Leu-->Phe)."
    Morle L., Roux A.-F., Alloisio N., Pothier B., Starck J., Denoroy J., Morle F., Rudigoz R.-C., Forget B.G., Delaunay J., Godet J.
    J. Clin. Invest. 86:548-554(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 CULOZ VAL-46, VARIANT EL2 LYON PHE-49.
  25. "Spectrin Jendouba: an alpha II/31 spectrin variant that is associated with elliptocytosis and carries a mutation distant from the dimer self-association site."
    Alloisio N., Wilmotte R., Morle L., Baklouti F., Marechal J., Ducluzeau M.-T., Denoroy L., Feo C., Forget B.G., Kastally R., Delaunay J.
    Blood 80:809-815(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 JENDOUBA GLU-791.
  26. "Spectrin Tunis (Sp alpha I/78), an elliptocytogenic variant, is due to the CGG-->TGG codon change (Arg-->Trp) at position 35 of the alpha I domain."
    Morle L., Morle F., Roux A.-F., Godet J., Forget B.G., Denoroy L., Garbarz M., Dhermy D., Kastally R., Delaunay J.
    Blood 74:828-832(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 TUNIS TRP-41.
  27. "Mild elliptocytosis associated with the alpha 34 Arg-->Trp mutation in spectrin Genova (alpha I/74)."
    Perrotta S., del Giudice E.M., Alloisio N., Sciarratta G., Pinto L., Delaunay J., Cutillo S., Lolascon A.
    Blood 83:3346-3349(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 GENOVA TRP-34.
  28. "Spectrin Anastasia (alpha I/78): a new spectrin variant (alpha 45 Arg-->Thr) with moderate elliptocytogenic potential."
    Perrotta S., Iolascon A., de Angelis F., Pagano L., Colonna G., Cutillo S., del Giudice E.M.
    Br. J. Haematol. 89:933-936(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EL2 ANASTASIA THR-45.

Entry informationi

Entry nameiSPTA1_HUMAN
AccessioniPrimary (citable) accession number: P02549
Secondary accession number(s): Q15514
, Q5VYL1, Q5VYL2, Q6LDY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 178 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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