P11277 (SPTB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spectrin beta chain, erythrocytic

Alternative name(s):
Beta-I spectrin

Gene names

Name:	SPTB
Synonyms:	SPTB1

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	2137 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 nonhomologous chains, alpha and beta, which aggregate to form dimers, tetramers, and higher polymers.
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › cell cortex.
Post-translational modification	The first phosphorylation event occurs on Ser-2114, followed by Ser-2125, Ser-2123, Ser-2128, Ser-2117, and Thr-2110.
Involvement in disease	Elliptocytosis 3 (EL3) [MIM:182870]: 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.15 Ref.17 Ref.18 Ref.19 Spherocytosis 2 (SPH2) [MIM:182870]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH1 is characterized by severe hemolytic anemia. Inheritance is autosomal dominant. 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 2 CH (calponin-homology) domains. Contains 17 spectrin repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Elliptocytosis Hereditary hemolytic anemia
Domain	Repeat
Ligand	Actin-binding
Molecular function	Actin capping
PTM	Phosphoprotein
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 axon guidance Traceable author statement. Source: Reactome hemopoiesis 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
Cellular_component	cell surface Inferred from direct assay PubMed 10867799. Source: UniProtKB cytosol Traceable author statement. Source: Reactome intrinsic to internal side of plasma membrane Traceable author statement PubMed 10950304. Source: BHF-UCL protein complex Inferred from direct assay PubMed 16060676. Source: UniProtKB spectrin Traceable author statement Ref.15. Source: ProtInc spectrin-associated cytoskeleton Inferred from direct assay PubMed 379653. Source: BHF-UCL
Molecular_function	actin filament binding Inferred from direct assay PubMed 16060676. Source: UniProtKB structural constituent of cytoskeleton Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SNAPIN	O95295	3	EBI-514908,EBI-296723

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P11277-1)

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: P11277-2)

Also known as: Muscle-specific;

The sequence of this isoform differs from the canonical sequence as follows:
     2116-2137: VSLWSRLSSSWESLQPEPSHPY → GEEEGTWPQN...KRFSFFPKKK

Isoform 3 (identifier: P11277-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2074-2137: LELKERQIAE...SLQPEPSHPY → ASRGGRRDSRGGSSFPPCGHRENVPGQSLVSFV

Note: Due to exon skipping.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 2137

2136

Spectrin beta chain, erythrocytic

PRO_0000073459

Regions

Domain

2 – 275

274

Actin-binding

Domain

54 – 158

105

CH 1

Domain

173 – 275

103

CH 2

Repeat

276 – 384

109

Spectrin 1

Repeat

385 – 498

114

Spectrin 2

Repeat

499 – 607

109

Spectrin 3

Repeat

608 – 713

106

Spectrin 4

Repeat

714 – 818

105

Spectrin 5

Repeat

819 – 924

106

Spectrin 6

Repeat

925 – 1031

107

Spectrin 7

Repeat

1032 – 1138

107

Spectrin 8

Repeat

1139 – 1244

106

Spectrin 9

Repeat

1245 – 1349

105

Spectrin 10

Repeat

1350 – 1455

106

Spectrin 11

Repeat

1456 – 1554

99

Spectrin 12

Repeat

1555 – 1660

106

Spectrin 13

Repeat

1661 – 1767

107

Spectrin 14

Repeat

1768 – 1873

106

Spectrin 15

Repeat

1874 – 1979

106

Spectrin 16

Repeat

1980 – 2085

106

Spectrin 17

Amino acid modifications

Modified residue

36

1

Phosphoserine By similarity

Modified residue

2110

1

Phosphothreonine Ref.11

Modified residue

2114

1

Phosphoserine Ref.11

Modified residue

2117

1

Phosphoserine Ref.11

Modified residue

2123

1

Phosphoserine Ref.11

Modified residue

2125

1

Phosphoserine Ref.11

Modified residue

2128

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

2074 – 2137

64

LELKE…PSHPY → ASRGGRRDSRGGSSFPPCGH RENVPGQSLVSFV in isoform 3.

VSP_007242

Alternative sequence

2116 – 2137

22

VSLWS…PSHPY → GEEEGTWPQNLQQPPPPGQH KDGQKSTGDERPTTEPLFKV LDTPLSEGDEPATLPAPRDH GQSVQMEGYLGRKHDLEGPN KKASNRSWNNLYCVLRNSEL TFYKDAKNLALGMPYHGEEP LALRHAICEIAANYKKKKHV FKLRLSNGSEWLFHGKDEEE MLSWLQGVSTAINESQSIRV KAQSLPLPSLSGPDASLGKK DKEKRFSFFPKKK in isoform 2.

VSP_000719

Natural variant

202

1

W → R in HS; Kissimmee. Ref.16

VAR_001352

Natural variant

439

1

S → N. Ref.1
Corresponds to variant rs229587 [ dbSNP | Ensembl ].

VAR_001353

Natural variant

525

1

E → K.
Corresponds to variant rs55752508 [ dbSNP | Ensembl ].

VAR_061084

Natural variant

613

1

S → I.
Corresponds to variant rs3742601 [ dbSNP | Ensembl ].

VAR_038514

Natural variant

1151

1

N → D. Ref.1 Ref.4 Ref.6
Corresponds to variant rs77806 [ dbSNP | Ensembl ].

VAR_001354

Natural variant

1374

1

H → R. Ref.7
Corresponds to variant rs10132778 [ dbSNP | Ensembl ].

VAR_001355

Natural variant

1403

1

R → Q.
Corresponds to variant rs17180350 [ dbSNP | Ensembl ].

VAR_001356

Natural variant

1408

1

G → R.
Corresponds to variant rs17245552 [ dbSNP | Ensembl ].

VAR_038515

Natural variant

2018

1

A → G in EL3; Cagliary. Ref.15

VAR_001357

Natural variant

2019

1

S → P in EL3; Providence. Ref.17

VAR_001358

Natural variant

2023

1

A → V in EL3; Paris. Ref.18

VAR_001359

Natural variant

2024

1

W → R in EL3; Linguere. Ref.18

VAR_001360

Natural variant

2025

1

L → R in EL3; Buffalo.

VAR_001361

Natural variant

2053

1

A → P in EL3; Kayes. Ref.19

VAR_001362

Experimental info

Sequence conflict

403

1

E → G in AAA60578. Ref.1

Sequence conflict

403

1

E → G in AAA60579. Ref.1

Sequence conflict

612

1

I → M in AAA60578. Ref.1

Sequence conflict

612

1

I → M in AAA60579. Ref.1

Sequence conflict

629 – 631

3

RKA → ART in AAA60578. Ref.1

Sequence conflict

629 – 631

3

RKA → ART in AAA60579. Ref.1

Sequence conflict

958 – 959

2

NY → TL in AAA60578. Ref.1

Sequence conflict

958 – 959

2

NY → TL in AAA60579. Ref.1

Sequence conflict

1031

1

D → N in AAA60578. Ref.1

Sequence conflict

1031

1

D → N in AAA60579. Ref.1

Sequence conflict

1844 – 1845

2

EL → DV in AAA60578. Ref.1

Sequence conflict

1844 – 1845

2

EL → DV in AAA60579. Ref.1

Sequence conflict

1844 – 1845

2

EL → DV in AAA63259. Ref.3

Secondary structure

1

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2137

Helix Strand Turn

Details...

Helix

1065 – 1085

21

Helix

1093 – 1128

36

Helix

1134 – 1192

59

Helix

1200 – 1236

37

Helix

1242 – 1271

30

Helix

1586 – 1605

20

Helix

1616 – 1652

37

Helix

1692 – 1713

22

Helix

1722 – 1759

38

Helix

1765 – 1818

54

Helix

1838 – 1863

26

Helix

1868 – 1891

24

Helix

1902 – 1928

27

Beta strand

1936 – 1938

3

Helix

1941 – 1971

31

Helix

1977 – 2033

57

Helix

2041 – 2060

20

Helix

2062 – 2069

8

Helix

2073 – 2082

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 5. Checksum: 311AE5CD53237610	FASTA	2,137	246,468
	10 20 30 40 50 60 MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF 70 80 90 100 110 120 TKWVNSHLAR VSCRITDLYK DLRDGRMLIK LLEVLSGEML PKPTKGKMRI HCLENVDKAL 130 140 150 160 170 180 QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVQTQEGR ETRSAKDALL 190 200 210 220 230 240 LWCQMKTAGY PHVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFNV 250 260 270 280 290 300 AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET 310 320 330 340 350 360 EKMIEKYSGL ASDLLTWIEQ TITVLNSRKF ANSLTGVQQQ LQAFSTYRTV EKPPKFQEKG 370 380 390 400 410 420 NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYRRELAL RNELIRQEKL 430 440 450 460 470 480 EQLARRFDRK AAMRETWLSE NQRLVAQDNF GYDLAAVEAA KKKHEAIETD TAAYEERVRA 490 500 510 520 530 540 LEDLAQELEK ENYHDQKRIT ARKDNILRLW SYLQELLQSR RQRLETTLAL QKLFQDMLHS 550 560 570 580 590 600 IDWMDEIKAH LLSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVKAITAA TLKFTEGKGY 610 620 630 640 650 660 QPCDPQVIQD RISHLEQCFE ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE SWIKEKEQIY 670 680 690 700 710 720 SSLDYGKDLT SVLILQRKHK AFEDELRGLD AHLEQIFQEA HGMVARKQFG HPQIEARIKE 730 740 750 760 770 780 VSAQWDQLKD LAAFCKKNLQ DAENFFQFQG DADDLKAWLQ DAHRLLSGED VGQDEGATRA 790 800 810 820 830 840 LGKKHKDFLE ELEESRGVME HLEQQAQGFP EEFRDSPDVT HRLQALRELY QQVVAQADLR 850 860 870 880 890 900 QQRLQEALDL YTVFGETDAC ELWMGEKEKW LAEMEMPDTL EDLEVVQHRF DILDQEMKTL 910 920 930 940 950 960 MTQIDGVNLA ANSLVESGHP RSREVKQYQD HLNTRWQAFQ TLVSERREAV DSALRVHNYC 970 980 990 1000 1010 1020 VDCEETSKWI TDKTKVVEST KDLGRDLAGI IAIQRKLSGL ERDVAAIQAR VDALERESQQ 1030 1040 1050 1060 1070 1080 LMDSHPEQKE DIGQRQKHLE ELWQGLQQSL QGQEDLLGEV SQLQAFLQDL DDFQAWLSIT 1090 1100 1110 1120 1130 1140 QKAVASEDMP ESLPEAEQLL QQHAGIKDEI DGHQDSYQRV KESGEKVIQG QTDPEYLLLG 1150 1160 1170 1180 1190 1200 QRLEGLDTGW NALGRMWESR SHTLAQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL 1210 1220 1230 1240 1250 1260 EAAEAGIRKF EDFLGSMENN RDKVLSPVDS GNKLVAEGNL YSDKIKEKVQ LIEDRHRKNN 1270 1280 1290 1300 1310 1320 EKAQEASVLL RDNLELQNFL QNCQELTLWI NDKLLTSQDV SYDEARNLHN KWLKHQAFVA 1330 1340 1350 1360 1370 1380 ELASHEGWLE NIDAEGKQLM DEKPQFTALV SQKLEALHRL WDELQATTKE KTQHLSAARS 1390 1400 1410 1420 1430 1440 SDLRLQTHAD LNKWISAMED QLRSDDPGKD LTSVNRMLAK LKRVEDQVNV RKEELGELFA 1450 1460 1470 1480 1490 1500 QVPSMGEEGG DADLSIEKRF LDLLEPLGRR KKQLESSRAK LQISRDLEDE TLWVEERLPL 1510 1520 1530 1540 1550 1560 AQSADYGTNL QTVQLFMKKN QTLQNEILGH TPRVEDVLQR GQQLVEAAEI DCQDLEERLG 1570 1580 1590 1600 1610 1620 HLQSSWDRLR EAAAGRLQRL RDANEAQQYY LDADEAEAWI GEQELYVISD EIPKDEEGAI 1630 1640 1650 1660 1670 1680 VMLKRHLRQQ RAVEDYGRNI KQLASRAQGL LSAGHPEGEQ IIRLQGQVDK HYAGLKDVAE 1690 1700 1710 1720 1730 1740 ERKRKLENMY HLFQLKRETD DLEQWISEKE LVASSPEMGQ DFDHVTLLRD KFRDFARETG 1750 1760 1770 1780 1790 1800 AIGQERVDNV NAFIERLIDA GHSEAATIAE WKDGLNEMWA DLLELIDTRM QLLAASYDLH 1810 1820 1830 1840 1850 1860 RYFYTGAEIL GLIDEKHREL PEDVGLDAST AESFHRVHTA FERELHLLGV QVQQFQDVAT 1870 1880 1890 1900 1910 1920 RLQTAYAGEK AEAIQNKEQE VSAAWQALLD ACAGRRTQLV DTADKFRFFS MARDLLSWME 1930 1940 1950 1960 1970 1980 SIIRQIETQE RPRDVSSVEL LMKYHQGINA EIETRSKNFS ACLELGESLL QRQHQASEEI 1990 2000 2010 2020 2030 2040 REKLQQVMSR RKEMNEKWEA RWERLRMLLE VCQFSRDASV AEAWLIAQEP YLASGDFGHT 2050 2060 2070 2080 2090 2100 VDSVEKLIKR HEAFEKSTAS WAERFAALEK PTTLELKERQ IAERPAEETG PQEEEGETAG 2110 2120 2130 EAPVSHHAAT ERTSPVSLWS RLSSSWESLQ PEPSHPY
	Isoform 2 (Muscle-specific) [UniParc]. Checksum: 5C3709E99F70B8D0	FASTA	2,328	267,826
	10 20 30 40 50 60 MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF 70 80 90 100 110 120 TKWVNSHLAR VSCRITDLYK DLRDGRMLIK LLEVLSGEML PKPTKGKMRI HCLENVDKAL 130 140 150 160 170 180 QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVQTQEGR ETRSAKDALL 190 200 210 220 230 240 LWCQMKTAGY PHVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFNV 250 260 270 280 290 300 AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET 310 320 330 340 350 360 EKMIEKYSGL ASDLLTWIEQ TITVLNSRKF ANSLTGVQQQ LQAFSTYRTV EKPPKFQEKG 370 380 390 400 410 420 NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYRRELAL RNELIRQEKL 430 440 450 460 470 480 EQLARRFDRK AAMRETWLSE NQRLVAQDNF GYDLAAVEAA KKKHEAIETD TAAYEERVRA 490 500 510 520 530 540 LEDLAQELEK ENYHDQKRIT ARKDNILRLW SYLQELLQSR RQRLETTLAL QKLFQDMLHS 550 560 570 580 590 600 IDWMDEIKAH LLSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVKAITAA TLKFTEGKGY 610 620 630 640 650 660 QPCDPQVIQD RISHLEQCFE ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE SWIKEKEQIY 670 680 690 700 710 720 SSLDYGKDLT SVLILQRKHK AFEDELRGLD AHLEQIFQEA HGMVARKQFG HPQIEARIKE 730 740 750 760 770 780 VSAQWDQLKD LAAFCKKNLQ DAENFFQFQG DADDLKAWLQ DAHRLLSGED VGQDEGATRA 790 800 810 820 830 840 LGKKHKDFLE ELEESRGVME HLEQQAQGFP EEFRDSPDVT HRLQALRELY QQVVAQADLR 850 860 870 880 890 900 QQRLQEALDL YTVFGETDAC ELWMGEKEKW LAEMEMPDTL EDLEVVQHRF DILDQEMKTL 910 920 930 940 950 960 MTQIDGVNLA ANSLVESGHP RSREVKQYQD HLNTRWQAFQ TLVSERREAV DSALRVHNYC 970 980 990 1000 1010 1020 VDCEETSKWI TDKTKVVEST KDLGRDLAGI IAIQRKLSGL ERDVAAIQAR VDALERESQQ 1030 1040 1050 1060 1070 1080 LMDSHPEQKE DIGQRQKHLE ELWQGLQQSL QGQEDLLGEV SQLQAFLQDL DDFQAWLSIT 1090 1100 1110 1120 1130 1140 QKAVASEDMP ESLPEAEQLL QQHAGIKDEI DGHQDSYQRV KESGEKVIQG QTDPEYLLLG 1150 1160 1170 1180 1190 1200 QRLEGLDTGW NALGRMWESR SHTLAQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL 1210 1220 1230 1240 1250 1260 EAAEAGIRKF EDFLGSMENN RDKVLSPVDS GNKLVAEGNL YSDKIKEKVQ LIEDRHRKNN 1270 1280 1290 1300 1310 1320 EKAQEASVLL RDNLELQNFL QNCQELTLWI NDKLLTSQDV SYDEARNLHN KWLKHQAFVA 1330 1340 1350 1360 1370 1380 ELASHEGWLE NIDAEGKQLM DEKPQFTALV SQKLEALHRL WDELQATTKE KTQHLSAARS 1390 1400 1410 1420 1430 1440 SDLRLQTHAD LNKWISAMED QLRSDDPGKD LTSVNRMLAK LKRVEDQVNV RKEELGELFA 1450 1460 1470 1480 1490 1500 QVPSMGEEGG DADLSIEKRF LDLLEPLGRR KKQLESSRAK LQISRDLEDE TLWVEERLPL 1510 1520 1530 1540 1550 1560 AQSADYGTNL QTVQLFMKKN QTLQNEILGH TPRVEDVLQR GQQLVEAAEI DCQDLEERLG 1570 1580 1590 1600 1610 1620 HLQSSWDRLR EAAAGRLQRL RDANEAQQYY LDADEAEAWI GEQELYVISD EIPKDEEGAI 1630 1640 1650 1660 1670 1680 VMLKRHLRQQ RAVEDYGRNI KQLASRAQGL LSAGHPEGEQ IIRLQGQVDK HYAGLKDVAE 1690 1700 1710 1720 1730 1740 ERKRKLENMY HLFQLKRETD DLEQWISEKE LVASSPEMGQ DFDHVTLLRD KFRDFARETG 1750 1760 1770 1780 1790 1800 AIGQERVDNV NAFIERLIDA GHSEAATIAE WKDGLNEMWA DLLELIDTRM QLLAASYDLH 1810 1820 1830 1840 1850 1860 RYFYTGAEIL GLIDEKHREL PEDVGLDAST AESFHRVHTA FERELHLLGV QVQQFQDVAT 1870 1880 1890 1900 1910 1920 RLQTAYAGEK AEAIQNKEQE VSAAWQALLD ACAGRRTQLV DTADKFRFFS MARDLLSWME 1930 1940 1950 1960 1970 1980 SIIRQIETQE RPRDVSSVEL LMKYHQGINA EIETRSKNFS ACLELGESLL QRQHQASEEI 1990 2000 2010 2020 2030 2040 REKLQQVMSR RKEMNEKWEA RWERLRMLLE VCQFSRDASV AEAWLIAQEP YLASGDFGHT 2050 2060 2070 2080 2090 2100 VDSVEKLIKR HEAFEKSTAS WAERFAALEK PTTLELKERQ IAERPAEETG PQEEEGETAG 2110 2120 2130 2140 2150 2160 EAPVSHHAAT ERTSPGEEEG TWPQNLQQPP PPGQHKDGQK STGDERPTTE PLFKVLDTPL 2170 2180 2190 2200 2210 2220 SEGDEPATLP APRDHGQSVQ MEGYLGRKHD LEGPNKKASN RSWNNLYCVL RNSELTFYKD 2230 2240 2250 2260 2270 2280 AKNLALGMPY HGEEPLALRH AICEIAANYK KKKHVFKLRL SNGSEWLFHG KDEEEMLSWL 2290 2300 2310 2320 QGVSTAINES QSIRVKAQSL PLPSLSGPDA SLGKKDKEKR FSFFPKKK
	Isoform 3 [UniParc]. Checksum: E48305033176AE98	FASTA	2,106	242,802
	10 20 30 40 50 60 MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF 70 80 90 100 110 120 TKWVNSHLAR VSCRITDLYK DLRDGRMLIK LLEVLSGEML PKPTKGKMRI HCLENVDKAL 130 140 150 160 170 180 QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVQTQEGR ETRSAKDALL 190 200 210 220 230 240 LWCQMKTAGY PHVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFNV 250 260 270 280 290 300 AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET 310 320 330 340 350 360 EKMIEKYSGL ASDLLTWIEQ TITVLNSRKF ANSLTGVQQQ LQAFSTYRTV EKPPKFQEKG 370 380 390 400 410 420 NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYRRELAL RNELIRQEKL 430 440 450 460 470 480 EQLARRFDRK AAMRETWLSE NQRLVAQDNF GYDLAAVEAA KKKHEAIETD TAAYEERVRA 490 500 510 520 530 540 LEDLAQELEK ENYHDQKRIT ARKDNILRLW SYLQELLQSR RQRLETTLAL QKLFQDMLHS 550 560 570 580 590 600 IDWMDEIKAH LLSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVKAITAA TLKFTEGKGY 610 620 630 640 650 660 QPCDPQVIQD RISHLEQCFE ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE SWIKEKEQIY 670 680 690 700 710 720 SSLDYGKDLT SVLILQRKHK AFEDELRGLD AHLEQIFQEA HGMVARKQFG HPQIEARIKE 730 740 750 760 770 780 VSAQWDQLKD LAAFCKKNLQ DAENFFQFQG DADDLKAWLQ DAHRLLSGED VGQDEGATRA 790 800 810 820 830 840 LGKKHKDFLE ELEESRGVME HLEQQAQGFP EEFRDSPDVT HRLQALRELY QQVVAQADLR 850 860 870 880 890 900 QQRLQEALDL YTVFGETDAC ELWMGEKEKW LAEMEMPDTL EDLEVVQHRF DILDQEMKTL 910 920 930 940 950 960 MTQIDGVNLA ANSLVESGHP RSREVKQYQD HLNTRWQAFQ TLVSERREAV DSALRVHNYC 970 980 990 1000 1010 1020 VDCEETSKWI TDKTKVVEST KDLGRDLAGI IAIQRKLSGL ERDVAAIQAR VDALERESQQ 1030 1040 1050 1060 1070 1080 LMDSHPEQKE DIGQRQKHLE ELWQGLQQSL QGQEDLLGEV SQLQAFLQDL DDFQAWLSIT 1090 1100 1110 1120 1130 1140 QKAVASEDMP ESLPEAEQLL QQHAGIKDEI DGHQDSYQRV KESGEKVIQG QTDPEYLLLG 1150 1160 1170 1180 1190 1200 QRLEGLDTGW NALGRMWESR SHTLAQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL 1210 1220 1230 1240 1250 1260 EAAEAGIRKF EDFLGSMENN RDKVLSPVDS GNKLVAEGNL YSDKIKEKVQ LIEDRHRKNN 1270 1280 1290 1300 1310 1320 EKAQEASVLL RDNLELQNFL QNCQELTLWI NDKLLTSQDV SYDEARNLHN KWLKHQAFVA 1330 1340 1350 1360 1370 1380 ELASHEGWLE NIDAEGKQLM DEKPQFTALV SQKLEALHRL WDELQATTKE KTQHLSAARS 1390 1400 1410 1420 1430 1440 SDLRLQTHAD LNKWISAMED QLRSDDPGKD LTSVNRMLAK LKRVEDQVNV RKEELGELFA 1450 1460 1470 1480 1490 1500 QVPSMGEEGG DADLSIEKRF LDLLEPLGRR KKQLESSRAK LQISRDLEDE TLWVEERLPL 1510 1520 1530 1540 1550 1560 AQSADYGTNL QTVQLFMKKN QTLQNEILGH TPRVEDVLQR GQQLVEAAEI DCQDLEERLG 1570 1580 1590 1600 1610 1620 HLQSSWDRLR EAAAGRLQRL RDANEAQQYY LDADEAEAWI GEQELYVISD EIPKDEEGAI 1630 1640 1650 1660 1670 1680 VMLKRHLRQQ RAVEDYGRNI KQLASRAQGL LSAGHPEGEQ IIRLQGQVDK HYAGLKDVAE 1690 1700 1710 1720 1730 1740 ERKRKLENMY HLFQLKRETD DLEQWISEKE LVASSPEMGQ DFDHVTLLRD KFRDFARETG 1750 1760 1770 1780 1790 1800 AIGQERVDNV NAFIERLIDA GHSEAATIAE WKDGLNEMWA DLLELIDTRM QLLAASYDLH 1810 1820 1830 1840 1850 1860 RYFYTGAEIL GLIDEKHREL PEDVGLDAST AESFHRVHTA FERELHLLGV QVQQFQDVAT 1870 1880 1890 1900 1910 1920 RLQTAYAGEK AEAIQNKEQE VSAAWQALLD ACAGRRTQLV DTADKFRFFS MARDLLSWME 1930 1940 1950 1960 1970 1980 SIIRQIETQE RPRDVSSVEL LMKYHQGINA EIETRSKNFS ACLELGESLL QRQHQASEEI 1990 2000 2010 2020 2030 2040 REKLQQVMSR RKEMNEKWEA RWERLRMLLE VCQFSRDASV AEAWLIAQEP YLASGDFGHT 2050 2060 2070 2080 2090 2100 VDSVEKLIKR HEAFEKSTAS WAERFAALEK PTTASRGGRR DSRGGSSFPP CGHRENVPGQ SLVSFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Full-length sequence of the cDNA for human erythroid beta-spectrin." Winkelmann J.C., Chang J.G., Tse W.T., Scarpa A.L., Marchesi V.T., Forget B.G. J. Biol. Chem. 265:11827-11832(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANTS ASN-439 AND ASP-1151.
[2]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation." Garbarz M., Tse W.T., Gallagher P.G., Picat C., Lecomte M.C., Galibert F., Dhermy D., Forget B.G. J. Clin. Invest. 88:76-81(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING.
[4]	"Beta spectrin in human skeletal muscle. Tissue-specific differential processing of 3' beta spectrin pre-mRNA generates a beta spectrin isoform with a unique carboxyl terminus." Winkelmann J.C., Costa F.F., Linzie B.L., Forget B.G. J. Biol. Chem. 265:20449-20454(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1055-2137 (ISOFORM 2), VARIANT ASP-1151. Tissue: Skeletal muscle.
[5]	"A splice site mutation of the beta-spectrin gene causing exon skipping in hereditary elliptocytosis associated with a truncated beta-spectrin chain." Gallagher P.G., Tse W.T., Costa F., Scarpa A., Boivin P., Delaunay J., Forget B.G. J. Biol. Chem. 266:15154-15159(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2002-2137 (ISOFORM 1).
[6]	"Identification of an unusual deletion within homologous repeats of human reticulocyte beta-spectrin and probable peptide polymorphism." Yoon S.H., Kentros C.G., Prchal J.T. Gene 91:297-302(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 928-1756 (ISOFORMS 1/2/3), VARIANT ASP-1151.
[7]	"Molecular cloning of the cDNA for human erythrocyte beta-spectrin." Winkelmann J.C., Leto T.L., Watkins P.C., Eddy R., Shows T.B., Linnenbach A.J., Sahr K.E., Kathuria N., Marchesi V.T., Forget B.G. Blood 72:328-334(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1334-1432 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE [MRNA] OF 1909-2137 (ISOFORM 1), VARIANT ARG-1374.
[8]	"Isolation and characterization of cDNA clones for human erythrocyte beta-spectrin." Prchal J.T., Morley B.J., Yoon S.-H., Coetzer T.L., Palek J., Conboy J.G., Kan Y.W. Proc. Natl. Acad. Sci. U.S.A. 84:7468-7472(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1209-1482 (ISOFORMS 1/2/3).
[9]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-18. Tissue: Platelet.
[10]	"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: DOMAINS.
[11]	"In vivo phosphorylation of human erythrocyte spectrin occurs in a sequential manner." Tang H.Y., Speicher D.W. Biochemistry 43:4251-4262(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-2110; SER-2114; SER-2117; SER-2123; SER-2125 AND SER-2128.
[12]	"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].
[13]	"Structural insights into the stability and flexibility of unusual erythroid spectrin repeats." Kusunoki H., MacDonald R.I., Mondragon A. Structure 12:645-656(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1064-1275.
[14]	"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.
[15]	"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 EL3 CAGLIARI GLY-2018.
[16]	"Beta spectrin Kissimmee: a spectrin variant associated with autosomal dominant hereditary spherocytosis and defective binding to protein 4.1." Becker P.S., Tse W.T., Lux S.E., Forget B.G. J. Clin. Invest. 92:612-616(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HS KISSIMMEE ARG-202.
[17]	"Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene." Gallagher P.G., Weed S.A., Tse W.T., Benoit L., Morrow J.S., Marchesi S.L., Mohandas N., Forget B.G. J. Clin. Invest. 95:1174-1182(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EL3 PROVIDENCE PRO-2019.
[18]	"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: VARIANTS EL3 VAL-2023 AND ARG-2024.
[19]	"Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association." Tse W.T., Lecomte M.-C., Costa F.F., Garbarz M., Feo C., Boivin P., Dhermy D., Forget B.G. J. Clin. Invest. 86:909-916(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EL3 PRO-2053.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J05500 mRNA. Translation: AAA60578.1.
J05500 mRNA. Translation: AAA60579.1.
AL121774 Genomic DNA. No translation available.
M37884 mRNA. Translation: AAA63259.1.
M37885 mRNA. Translation: AAA60571.1.
M57948 mRNA. No translation available.
X59510 mRNA. Translation: CAA42097.1.
X59511 mRNA. Translation: CAA42098.1.
M18054 mRNA. Translation: AAA60572.1.

IPI

IPI00216704.
IPI00237806.
IPI00783228.

PIR

SJHUB. A37064.

RefSeq

NP_000338.3. NM_000347.5.
NP_001020029.1. NM_001024858.2.

UniGene

Hs.417303.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1S35	X-ray	2.40	A	1064-1275	[»]
3EDU	X-ray	2.10	A	1692-1907	[»]
3F57	X-ray	2.90	A/B	1686-1907	[»]
3KBT	X-ray	2.75	A/B	1583-1906	[»]
3KBU	X-ray	2.75	A/B	1583-1906	[»]
3LBX	X-ray	2.80	B	1902-2084	[»]

ProteinModelPortal

P11277.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1021N.

IntAct

P11277. 6 interactions.

MINT

MINT-3007632.

STRING

9606.ENSP00000374372.

PTM databases

PhosphoSite

P11277.

Polymorphism databases

DMDM

215274269.

2D gel databases

SWISS-2DPAGE

P11277.

Proteomic databases

PaxDb

P11277.

PRIDE

P11277.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000389720; ENSP00000374370; ENSG00000070182.
ENST00000389721; ENSP00000374371; ENSG00000070182.
ENST00000389722; ENSP00000374372; ENSG00000070182.
ENST00000542895; ENSP00000443882; ENSG00000070182.
ENST00000556626; ENSP00000451752; ENSG00000070182.

GeneID

6710.

KEGG

hsa:6710.

UCSC

uc001xhr.3. human.
uc001xht.3. human.

Organism-specific databases

CTD

6710.

GeneCards

GC14M065213.

HGNC

HGNC:11274. SPTB.

HPA

CAB015169.
HPA003394.
HPA003398.

MIM

130600. phenotype.
182870. gene+phenotype.

neXtProt

NX_P11277.

Orphanet

822. Hereditary spherocytosis.

PharmGKB

PA36103.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5069.

HOGENOM

HOG000007281.

HOVERGEN

HBG057912.

KO

K06115.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_127416. Developmental Biology.

Gene expression databases

ArrayExpress

P11277.

Bgee

P11277.

CleanEx

HS_SPTB.

Genevestigator

P11277.

GermOnline

ENSG00000070182. Homo sapiens.

Family and domain databases

Gene3D

1.10.418.10. 2 hits.

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]

Pfam

PF00307. CH. 2 hits.
PF00435. Spectrin. 17 hits.
[Graphical view]

PIRSF

PIRSF002297. Spectrin_beta_subunit. 1 hit.

SMART

SM00033. CH. 2 hits.
SM00150. SPEC. 17 hits.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P11277.

GenomeRNAi

6710.

NextBio

26166.

SOURCE

Search...

Entry information

Entry name

SPTB1_HUMAN

Accession

Primary (citable) accession number: P11277
Secondary accession number(s): Q15510, Q15519

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 25, 2008
Last modified:	May 29, 2013
This is version 149 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.