P02549 (SPTA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spectrin alpha chain, erythrocytic 1

Alternative name(s):
Erythroid alpha-spectrin

Gene names

Name:	SPTA1
Synonyms:	SPTA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2419 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Cytoplasm › cell 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 process	Cell shape
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Elliptocytosis Hereditary hemolytic anemia Pyropoikilocytosis
Domain	Repeat SH3 domain
Ligand	Actin-binding Calcium Metal-binding
Molecular function	Actin capping
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin 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: Compara lymphocyte homeostasis Inferred from electronic annotation. Source: Compara plasma membrane organization Inferred from electronic annotation. Source: Compara porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of protein binding Inferred from electronic annotation. Source: Compara regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cuticular plate Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome intrinsic to internal side of 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_function	actin filament binding Traceable author statement Ref.9. Source: ProtInc calcium ion binding Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton Traceable author statement Ref.9. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABI1	Q8IZP0	2	EBI-375617,EBI-375446
SPTBN1	Q01082	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2419

2419

Spectrin alpha chain, erythrocytic 1

PRO_0000073452

Regions

Repeat

19 – 51

33

Spectrin 1

Repeat

53 – 156

104

Spectrin 2

Repeat

158 – 262

105

Spectrin 3

Repeat

264 – 368

105

Spectrin 4

Repeat

370 – 474

105

Spectrin 5

Repeat

476 – 580

105

Spectrin 6

Repeat

582 – 685

104

Spectrin 7

Repeat

687 – 791

105

Spectrin 8

Repeat

793 – 897

105

Spectrin 9

Repeat

899 – 968

70

Spectrin 10

Domain

977 – 1036

60

SH3

Repeat

1082 – 1181

100

Spectrin 11

Repeat

1183 – 1287

105

Spectrin 12

Repeat

1289 – 1393

105

Spectrin 13

Repeat

1395 – 1498

104

Spectrin 14

Repeat

1500 – 1605

106

Spectrin 15

Repeat

1607 – 1711

105

Spectrin 16

Repeat

1713 – 1817

105

Spectrin 17

Repeat

1819 – 1926

108

Spectrin 18

Repeat

1928 – 2033

106

Spectrin 19

Repeat

2043 – 2147

105

Spectrin 20

Repeat

2157 – 2258

102

Spectrin 21

Domain

2271 – 2306

36

EF-hand 1

Domain

2314 – 2349

36

EF-hand 2

Domain

2352 – 2386

35

EF-hand 3

Calcium binding

2284 – 2295

12

1 Potential

Calcium binding

2327 – 2338

12

2 Potential

Natural variations

Alternative sequence

1889 – 1891

3

Missing in isoform 2.

VSP_037662

Natural variant

24

1

I → S in EL2; Lograno. Ref.16

VAR_001324

Natural variant

28

1

R → C in EL2. Ref.17

VAR_001328

Natural variant

28

1

R → H in EL2; Corbeil. Ref.17
Corresponds to variant rs28934004 [ dbSNP | Ensembl ].

VAR_001325

Natural variant

28

1

R → L in EL2. Ref.17

VAR_001326

Natural variant

28

1

R → S in EL2. Ref.17 Ref.18
Corresponds to variant rs28934005 [ dbSNP | Ensembl ].

VAR_001327

Natural variant

31

1

V → A in EL2; Marseille.

VAR_001329

Natural variant

34

1

R → W in EL2; Genova. Ref.27

VAR_001330

Natural variant

41

1

R → W in EL2; Tunis. Ref.26

VAR_001331

Natural variant

45

1

R → S in EL2; Clichy. Ref.19

VAR_001332

Natural variant

45

1

R → T in EL2; Anastasia. Ref.28

VAR_001333

Natural variant

46

1

G → V in EL2; Culoz. Ref.24

VAR_001334

Natural variant

48

1

K → R in HPP. Ref.18

VAR_001335

Natural variant

49

1

L → F in EL2; Lyon. Ref.24

VAR_001336

Natural variant

109

1

S → F.
Corresponds to variant rs3737521 [ dbSNP | Ensembl ].

VAR_038506

Natural variant

151

1

G → D in EL2; Ponte de Sor.

VAR_001337

Natural variant

152

1

D → N.
Corresponds to variant rs16840544 [ dbSNP | Ensembl ].

VAR_038507

Natural variant

154

1

L → LL in EL2.

VAR_001338

Natural variant

207

1

L → P in EL2 and HPP; Saint-Louis. Ref.20

VAR_001339

Natural variant

260

1

L → P in EL2; Nigerian. Ref.3

VAR_001340

Natural variant

261

1

S → P in EL2. Ref.3

VAR_001341

Natural variant

469

1

H → P in EL2; Barcelona. Ref.22

VAR_001342

Natural variant

469

1

Missing in EL2; Alexandria.

VAR_001343

Natural variant

471

1

Q → P in EL2. Ref.3

VAR_001344

Natural variant

701

1

R → H.
Corresponds to variant rs12090314 [ dbSNP | Ensembl ].

VAR_001345

Natural variant

766

1

A → T.
Corresponds to variant rs11265047 [ dbSNP | Ensembl ].

VAR_038508

Natural variant

791

1

D → E in EL2; Jendouba. Ref.25
Corresponds to variant rs7418956 [ dbSNP | Ensembl ].

VAR_001346

Natural variant

809

1

I → V.
Corresponds to variant rs7547313 [ dbSNP | Ensembl ].

VAR_001347

Natural variant

853

1

T → R.
Corresponds to variant rs35121052 [ dbSNP | Ensembl ].

VAR_001348

Natural variant

957

1

A → V.
Corresponds to variant rs34706737 [ dbSNP | Ensembl ].

VAR_038509

Natural variant

970

1

A → D.
Corresponds to variant rs35948326 [ dbSNP | Ensembl ].

VAR_001349

Natural variant

1163

1

S → A. Ref.1
Corresponds to variant rs2482965 [ dbSNP | Ensembl ].

VAR_038510

Natural variant

1330

1

R → I.
Corresponds to variant rs34214405 [ dbSNP | Ensembl ].

VAR_038511

Natural variant

1568

1

C → R. Ref.1 Ref.7
Corresponds to variant rs863931 [ dbSNP | Ensembl ].

VAR_038512

Natural variant

1693

1

K → Q.
Corresponds to variant rs857725 [ dbSNP | Ensembl ].

VAR_059199

Natural variant

1836

1

N → S.
Corresponds to variant rs16830483 [ dbSNP | Ensembl ].

VAR_059200

Natural variant

1858

1

L → V. Ref.21
Corresponds to variant rs3737515 [ dbSNP | Ensembl ].

VAR_001350

Natural variant

2025

1

A → G in Cagliari. Ref.23

VAR_001351

Natural variant

2265

1

I → T.
Corresponds to variant rs952094 [ dbSNP | Ensembl ].

VAR_059201

Experimental info

Sequence conflict

119 – 130

12

Missing in AAA60575. Ref.3

Sequence conflict

395

1

A → G in AAA60575. Ref.3

Sequence conflict

1410

1

W → R in AAA60577. Ref.1

Sequence conflict

1410

1

W → R in AAA60994. Ref.1

Sequence conflict

1570

1

Missing in AAA60577. Ref.1

Sequence conflict

1570

1

Missing in AAA60994. Ref.1

Sequence conflict

1570

1

Missing in AAA60569. Ref.7

Sequence conflict

1891

1

Q → H in AAA60577. Ref.1

Sequence conflict

1891

1

Q → H in AAA60994. Ref.1

Sequence conflict

2400 – 2419

20

GRSHL…SYFGN → VEAISLAMTTLASPIPTLAT NKQLLVDRRKS in AAA60577. Ref.1

Sequence conflict

2400 – 2419

20

GRSHL…SYFGN → VEAISLAMTTLASPIPTLAT NKQLLVDRRKS in AAA60994. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

2419

Helix Strand Turn

Details...

Beta strand

12 – 14

3

Helix

24 – 26

3

Helix

27 – 30

4

Helix

31 – 33

3

Helix

34 – 77

44

Helix

87 – 118

32

Helix

126 – 156

31

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 5. Checksum: B60680145C58DF55	FASTA	2,419	280,014
	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
	Isoform 2 [UniParc]. Checksum: C3824332610EF99C	FASTA	2,416	279,674
	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 QGEDILNKEE SQNKEISSKI EALNEKTPSL AKAIAAWKLQ 1930 1940 1950 1960 1970 1980 LEDDYAFQEF NWKADVVEAW IADKETSLKT NGNGADLGDF LTLLAKQDTL DASLQSFQQE 1990 2000 2010 2020 2030 2040 RLPEITDLKD KLISAQHNQS KAIEERYAAL LKRWEQLLEA SAVHRQKLLE KQLPLQKAED 2050 2060 2070 2080 2090 2100 LFVEFAHKAS ALNNWCEKME ENLSEPVHCV SLNEIRQLQK DHEDFLASLA RAQADFKCLL 2110 2120 2130 2140 2150 2160 ELDQQIKALG VPSSPYTWLT VEVLERTWKH LSDIIEEREQ ELQKEEARQV KNFEMCQEFE 2170 2180 2190 2200 2210 2220 QNASTFLQWI LETRAYFLDG SLLKETGTLE SQLEANKRKQ KEIQAMKRQL TKIVDLGDNL 2230 2240 2250 2260 2270 2280 EDALILDIKY STIGLAQQWD QLYQLGLRMQ HNLEQQIQAK DIKGVSEETL KEFSTIYKHF 2290 2300 2310 2320 2330 2340 DENLTGRLTH KEFRSCLRGL NYYLPMVEED EHEPKFEKFL DAVDPGRKGY VSLEDYTAFL 2350 2360 2370 2380 2390 2400 IDKESENIKS SDEIENAFQA LAEGKSYITK EDMKQALTPE QVSFCATHMQ QYMDPRGRSH 2410 LSGYDYVGFT NSYFGN

References

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[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]	"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 , 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.

IPI

IPI00220741.
IPI00641363.

PIR

SJHUA. A35716.

RefSeq

NP_003117.2. NM_003126.2.

UniGene

Hs.119825.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OWA	NMR	-	A	1-156	[»]
3LBX	X-ray	2.80	A	1-158	[»]

ProteinModelPortal

P02549.

SMR

P02549. Positions 1-953, 993-1034, 1049-2264, 2275-2377.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1020N.
DIP-17031N.

IntAct

P02549. 8 interactions.

STRING

9606.ENSP00000357130.

PTM databases

PhosphoSite

P02549.

Polymorphism databases

DMDM

308153675.

Proteomic databases

PaxDb

P02549.

PRIDE

P02549.

Protocols and materials databases

DNASU

6708.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368147; ENSP00000357129; ENSG00000163554.
ENST00000368148; ENSP00000357130; ENSG00000163554.

GeneID

6708.

KEGG

hsa:6708.

UCSC

uc001fst.1. human.

Organism-specific databases

CTD

6708.

GeneCards

GC01M158580.

H-InvDB

HIX0028529.

HGNC

HGNC:11272. SPTA1.

HPA

HPA028048.

MIM

130600. phenotype.
182860. gene.
266140. phenotype.
270970. phenotype.

neXtProt

NX_P02549.

Orphanet

98864. Common hereditary elliptocytosis.
288. Hereditary elliptocytosis.
98867. Hereditary pyropoikilocytosis.
822. Hereditary spherocytosis.

PharmGKB

PA36101.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG237318.

HOGENOM

HOG000246965.

HOVERGEN

HBG059266.

InParanoid

P02549.

KO

K06114.

OMA

EFWLSEA.

OrthoDB

EOG4PC9R6.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_127416. Developmental Biology.

Gene expression databases

ArrayExpress

P02549.

Bgee

P02549.

CleanEx

HS_SPTA1.

Genevestigator

P02549.

GermOnline

ENSG00000163554. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.

InterPro

IPR011992. EF-hand-like_dom.
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]

Pfam

PF08726. efhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]

PRINTS

PR01887. SPECTRNALPHA.

SMART

SM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50222. EF_HAND_2. 3 hits.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SPTA1. human.

EvolutionaryTrace

P02549.

GenomeRNAi

6708.

NextBio

26158.

SOURCE

Search...

Entry information

Entry name

SPTA1_HUMAN

Accession

Primary (citable) accession number: P02549
Secondary accession number(s): Q15514 , Q5VYL1, Q5VYL2, Q6LDY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 163 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.