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Protein

Spectrin beta chain, erythrocytic

Gene

SPTB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

GO - Molecular functioni

  • actin binding Source: ProtInc
  • actin filament binding Source: UniProtKB
  • ankyrin binding Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000070182-MONOMER.
ReactomeiR-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain, erythrocytic
Alternative name(s):
Beta-I spectrin
Gene namesi
Name:SPTB
Synonyms:SPTB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:11274. SPTB.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: BHF-UCL
  • cell surface Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • intrinsic component of the cytoplasmic side of the plasma membrane Source: BHF-UCL
  • protein complex Source: UniProtKB
  • spectrin Source: ProtInc
  • spectrin-associated cytoskeleton Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Elliptocytosis 3 (EL3)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:182870
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0013572018A → G in EL3; Cagliary. 1 PublicationCorresponds to variant rs121918647dbSNPEnsembl.1
Natural variantiVAR_0013582019S → P in EL3; Providence. 1 PublicationCorresponds to variant rs121918648dbSNPEnsembl.1
Natural variantiVAR_0013592023A → V in EL3; Paris. 1 PublicationCorresponds to variant rs367841692dbSNPEnsembl.1
Natural variantiVAR_0013602024W → R in EL3; Linguere. 1 Publication1
Natural variantiVAR_0013612025L → R in EL3; Buffalo. Corresponds to variant rs121918649dbSNPEnsembl.1
Natural variantiVAR_0013622053A → P in EL3; Kayes. 1 PublicationCorresponds to variant rs121918645dbSNPEnsembl.1
Spherocytosis 2 (SPH2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of hereditary spherocytosis, a group of hematologic disorders characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. Clinical manifestations include chronic hemolytic anemia, jaundice, and splenomegaly, with variable severity.
See also OMIM:616649
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001352202W → R in SPH2; spectrin Kissimmee. 1 PublicationCorresponds to variant rs121918646dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Elliptocytosis, Hereditary hemolytic anemia

Organism-specific databases

DisGeNETi6710.
MalaCardsiSPTB.
MIMi182870. gene+phenotype.
616649. phenotype.
OpenTargetsiENSG00000070182.
Orphaneti288. Hereditary elliptocytosis.
822. Hereditary spherocytosis.
PharmGKBiPA36103.

Polymorphism and mutation databases

BioMutaiSPTB.
DMDMi215274269.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000734592 – 2137Spectrin beta chain, erythrocyticAdd BLAST2136

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36PhosphoserineBy similarity1
Modified residuei104PhosphothreonineCombined sources1
Modified residuei1297PhosphoserineBy similarity1
Modified residuei2043PhosphoserineCombined sources1
Modified residuei2073PhosphothreonineCombined sources1
Modified residuei2110Phosphothreonine1 Publication1
Modified residuei2114Phosphoserine1 Publication1
Modified residuei2117Phosphoserine1 Publication1
Modified residuei2123PhosphoserineCombined sources1 Publication1
Modified residuei2125PhosphoserineCombined sources1 Publication1
Modified residuei2128Phosphoserine1 Publication1

Post-translational modificationi

The first phosphorylation event occurs on Ser-2114, followed by Ser-2125, Ser-2123, Ser-2128, Ser-2117, and Thr-2110.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP11277.
MaxQBiP11277.
PaxDbiP11277.
PeptideAtlasiP11277.
PRIDEiP11277.

2D gel databases

SWISS-2DPAGEP11277.

PTM databases

iPTMnetiP11277.
PhosphoSitePlusiP11277.

Expressioni

Gene expression databases

BgeeiENSG00000070182.
CleanExiHS_SPTB.
ExpressionAtlasiP11277. baseline and differential.
GenevisibleiP11277. HS.

Organism-specific databases

HPAiCAB015169.
CAB016232.
HPA003394.
HPA003398.

Interactioni

Subunit structurei

Composed of nonhomologous chains, alpha and beta, which aggregate to form dimers, tetramers, and higher polymers.

Binary interactionsi

WithEntry#Exp.IntActNotes
SNAPINO952953EBI-514908,EBI-296723
SPTA1P025494EBI-514908,EBI-375617

GO - Molecular functioni

  • actin binding Source: ProtInc
  • actin filament binding Source: UniProtKB
  • ankyrin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112588. 22 interactors.
DIPiDIP-1021N.
IntActiP11277. 8 interactors.
MINTiMINT-3007632.
STRINGi9606.ENSP00000374372.

Structurei

Secondary structure

12137
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1065 – 1085Combined sources21
Helixi1093 – 1128Combined sources36
Helixi1134 – 1192Combined sources59
Helixi1200 – 1236Combined sources37
Helixi1242 – 1271Combined sources30
Helixi1586 – 1605Combined sources20
Helixi1616 – 1652Combined sources37
Helixi1692 – 1713Combined sources22
Helixi1722 – 1759Combined sources38
Helixi1765 – 1818Combined sources54
Helixi1838 – 1863Combined sources26
Helixi1868 – 1891Combined sources24
Helixi1902 – 1928Combined sources27
Beta strandi1936 – 1938Combined sources3
Helixi1941 – 1971Combined sources31
Helixi1977 – 2033Combined sources57
Helixi2041 – 2060Combined sources20
Helixi2062 – 2069Combined sources8
Helixi2073 – 2082Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S35X-ray2.40A1063-1275[»]
3EDUX-ray2.10A1692-1907[»]
3F57X-ray2.90A/B1686-1907[»]
3KBTX-ray2.75A/B1583-1906[»]
3KBUX-ray2.75A/B1583-1906[»]
3LBXX-ray2.80B1902-2084[»]
ProteinModelPortaliP11277.
SMRiP11277.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11277.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 275Actin-bindingAdd BLAST274
Domaini54 – 158CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini173 – 275CH 2PROSITE-ProRule annotationAdd BLAST103
Repeati276 – 384Spectrin 1Add BLAST109
Repeati385 – 498Spectrin 2Add BLAST114
Repeati499 – 607Spectrin 3Add BLAST109
Repeati608 – 713Spectrin 4Add BLAST106
Repeati714 – 818Spectrin 5Add BLAST105
Repeati819 – 924Spectrin 6Add BLAST106
Repeati925 – 1031Spectrin 7Add BLAST107
Repeati1032 – 1138Spectrin 8Add BLAST107
Repeati1139 – 1244Spectrin 9Add BLAST106
Repeati1245 – 1349Spectrin 10Add BLAST105
Repeati1350 – 1455Spectrin 11Add BLAST106
Repeati1456 – 1554Spectrin 12Add BLAST99
Repeati1555 – 1660Spectrin 13Add BLAST106
Repeati1661 – 1767Spectrin 14Add BLAST107
Repeati1768 – 1873Spectrin 15Add BLAST106
Repeati1874 – 1979Spectrin 16Add BLAST106
Repeati1980 – 2085Spectrin 17Add BLAST106

Sequence similaritiesi

Belongs to the spectrin family.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 17 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0517. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000007281.
HOVERGENiHBG057912.
InParanoidiP11277.
KOiK06115.
OMAiGSEWLFH.
OrthoDBiEOG091G003V.
PhylomeDBiP11277.
TreeFamiTF313446.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00435. Spectrin. 17 hits.
[Graphical view]
PIRSFiPIRSF002297. Spectrin_beta_subunit. 1 hit.
SMARTiSM00033. CH. 2 hits.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11277-1) [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

        10         20         30         40         50
MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD
60 70 80 90 100
EREVVQKKTF TKWVNSHLAR VSCRITDLYK DLRDGRMLIK LLEVLSGEML
110 120 130 140 150
PKPTKGKMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI
160 170 180 190 200
WTIILRFQIQ DIVVQTQEGR ETRSAKDALL LWCQMKTAGY PHVNVTNFTS
210 220 230 240 250
SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFNV AERQLGIIPL
260 270 280 290 300
LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET
310 320 330 340 350
EKMIEKYSGL ASDLLTWIEQ TITVLNSRKF ANSLTGVQQQ LQAFSTYRTV
360 370 380 390 400
EKPPKFQEKG NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE
410 420 430 440 450
EAEYRRELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVAQDNF
460 470 480 490 500
GYDLAAVEAA KKKHEAIETD TAAYEERVRA LEDLAQELEK ENYHDQKRIT
510 520 530 540 550
ARKDNILRLW SYLQELLQSR RQRLETTLAL QKLFQDMLHS IDWMDEIKAH
560 570 580 590 600
LLSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVKAITAA TLKFTEGKGY
610 620 630 640 650
QPCDPQVIQD RISHLEQCFE ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE
660 670 680 690 700
SWIKEKEQIY SSLDYGKDLT SVLILQRKHK AFEDELRGLD AHLEQIFQEA
710 720 730 740 750
HGMVARKQFG HPQIEARIKE VSAQWDQLKD LAAFCKKNLQ DAENFFQFQG
760 770 780 790 800
DADDLKAWLQ DAHRLLSGED VGQDEGATRA LGKKHKDFLE ELEESRGVME
810 820 830 840 850
HLEQQAQGFP EEFRDSPDVT HRLQALRELY QQVVAQADLR QQRLQEALDL
860 870 880 890 900
YTVFGETDAC ELWMGEKEKW LAEMEMPDTL EDLEVVQHRF DILDQEMKTL
910 920 930 940 950
MTQIDGVNLA ANSLVESGHP RSREVKQYQD HLNTRWQAFQ TLVSERREAV
960 970 980 990 1000
DSALRVHNYC VDCEETSKWI TDKTKVVEST KDLGRDLAGI IAIQRKLSGL
1010 1020 1030 1040 1050
ERDVAAIQAR VDALERESQQ LMDSHPEQKE DIGQRQKHLE ELWQGLQQSL
1060 1070 1080 1090 1100
QGQEDLLGEV SQLQAFLQDL DDFQAWLSIT QKAVASEDMP ESLPEAEQLL
1110 1120 1130 1140 1150
QQHAGIKDEI DGHQDSYQRV KESGEKVIQG QTDPEYLLLG QRLEGLDTGW
1160 1170 1180 1190 1200
NALGRMWESR SHTLAQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL
1210 1220 1230 1240 1250
EAAEAGIRKF EDFLGSMENN RDKVLSPVDS GNKLVAEGNL YSDKIKEKVQ
1260 1270 1280 1290 1300
LIEDRHRKNN EKAQEASVLL RDNLELQNFL QNCQELTLWI NDKLLTSQDV
1310 1320 1330 1340 1350
SYDEARNLHN KWLKHQAFVA ELASHEGWLE NIDAEGKQLM DEKPQFTALV
1360 1370 1380 1390 1400
SQKLEALHRL WDELQATTKE KTQHLSAARS SDLRLQTHAD LNKWISAMED
1410 1420 1430 1440 1450
QLRSDDPGKD LTSVNRMLAK LKRVEDQVNV RKEELGELFA QVPSMGEEGG
1460 1470 1480 1490 1500
DADLSIEKRF LDLLEPLGRR KKQLESSRAK LQISRDLEDE TLWVEERLPL
1510 1520 1530 1540 1550
AQSADYGTNL QTVQLFMKKN QTLQNEILGH TPRVEDVLQR GQQLVEAAEI
1560 1570 1580 1590 1600
DCQDLEERLG HLQSSWDRLR EAAAGRLQRL RDANEAQQYY LDADEAEAWI
1610 1620 1630 1640 1650
GEQELYVISD EIPKDEEGAI VMLKRHLRQQ RAVEDYGRNI KQLASRAQGL
1660 1670 1680 1690 1700
LSAGHPEGEQ IIRLQGQVDK HYAGLKDVAE ERKRKLENMY HLFQLKRETD
1710 1720 1730 1740 1750
DLEQWISEKE LVASSPEMGQ DFDHVTLLRD KFRDFARETG AIGQERVDNV
1760 1770 1780 1790 1800
NAFIERLIDA GHSEAATIAE WKDGLNEMWA DLLELIDTRM QLLAASYDLH
1810 1820 1830 1840 1850
RYFYTGAEIL GLIDEKHREL PEDVGLDAST AESFHRVHTA FERELHLLGV
1860 1870 1880 1890 1900
QVQQFQDVAT RLQTAYAGEK AEAIQNKEQE VSAAWQALLD ACAGRRTQLV
1910 1920 1930 1940 1950
DTADKFRFFS MARDLLSWME SIIRQIETQE RPRDVSSVEL LMKYHQGINA
1960 1970 1980 1990 2000
EIETRSKNFS ACLELGESLL QRQHQASEEI REKLQQVMSR RKEMNEKWEA
2010 2020 2030 2040 2050
RWERLRMLLE VCQFSRDASV AEAWLIAQEP YLASGDFGHT VDSVEKLIKR
2060 2070 2080 2090 2100
HEAFEKSTAS WAERFAALEK PTTLELKERQ IAERPAEETG PQEEEGETAG
2110 2120 2130
EAPVSHHAAT ERTSPVSLWS RLSSSWESLQ PEPSHPY
Length:2,137
Mass (Da):246,468
Last modified:November 25, 2008 - v5
Checksum:i311AE5CD53237610
GO
Isoform 2 (identifier: P11277-2) [UniParc]FASTAAdd to basket
Also known as: Muscle-specific

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

Show »
Length:2,328
Mass (Da):267,826
Checksum:i5C3709E99F70B8D0
GO
Isoform 3 (identifier: P11277-3) [UniParc]FASTAAdd to basket

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

Note: Due to exon skipping.
Show »
Length:2,106
Mass (Da):242,802
Checksum:iE48305033176AE98
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti403E → G in AAA60578 (PubMed:2195026).Curated1
Sequence conflicti403E → G in AAA60579 (PubMed:2195026).Curated1
Sequence conflicti612I → M in AAA60578 (PubMed:2195026).Curated1
Sequence conflicti612I → M in AAA60579 (PubMed:2195026).Curated1
Sequence conflicti629 – 631RKA → ART in AAA60578 (PubMed:2195026).Curated3
Sequence conflicti629 – 631RKA → ART in AAA60579 (PubMed:2195026).Curated3
Sequence conflicti958 – 959NY → TL in AAA60578 (PubMed:2195026).Curated2
Sequence conflicti958 – 959NY → TL in AAA60579 (PubMed:2195026).Curated2
Sequence conflicti1031D → N in AAA60578 (PubMed:2195026).Curated1
Sequence conflicti1031D → N in AAA60579 (PubMed:2195026).Curated1
Sequence conflicti1844 – 1845EL → DV in AAA60578 (PubMed:2195026).Curated2
Sequence conflicti1844 – 1845EL → DV in AAA60579 (PubMed:2195026).Curated2
Sequence conflicti1844 – 1845EL → DV in AAA63259 (PubMed:2056132).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001352202W → R in SPH2; spectrin Kissimmee. 1 PublicationCorresponds to variant rs121918646dbSNPEnsembl.1
Natural variantiVAR_001353439S → N.1 PublicationCorresponds to variant rs229587dbSNPEnsembl.1
Natural variantiVAR_061084525E → K.Corresponds to variant rs55752508dbSNPEnsembl.1
Natural variantiVAR_038514613S → I.Corresponds to variant rs3742601dbSNPEnsembl.1
Natural variantiVAR_0013541151N → D.3 PublicationsCorresponds to variant rs77806dbSNPEnsembl.1
Natural variantiVAR_0013551374H → R.1 PublicationCorresponds to variant rs10132778dbSNPEnsembl.1
Natural variantiVAR_0013561403R → Q.Corresponds to variant rs17180350dbSNPEnsembl.1
Natural variantiVAR_0385151408G → R.Corresponds to variant rs17245552dbSNPEnsembl.1
Natural variantiVAR_0013572018A → G in EL3; Cagliary. 1 PublicationCorresponds to variant rs121918647dbSNPEnsembl.1
Natural variantiVAR_0013582019S → P in EL3; Providence. 1 PublicationCorresponds to variant rs121918648dbSNPEnsembl.1
Natural variantiVAR_0013592023A → V in EL3; Paris. 1 PublicationCorresponds to variant rs367841692dbSNPEnsembl.1
Natural variantiVAR_0013602024W → R in EL3; Linguere. 1 Publication1
Natural variantiVAR_0013612025L → R in EL3; Buffalo. Corresponds to variant rs121918649dbSNPEnsembl.1
Natural variantiVAR_0013622053A → P in EL3; Kayes. 1 PublicationCorresponds to variant rs121918645dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0072422074 – 2137LELKE…PSHPY → ASRGGRRDSRGGSSFPPCGH RENVPGQSLVSFV in isoform 3. 1 PublicationAdd BLAST64
Alternative sequenceiVSP_0007192116 – 2137VSLWS…PSHPY → GEEEGTWPQNLQQPPPPGQH KDGQKSTGDERPTTEPLFKV LDTPLSEGDEPATLPAPRDH GQSVQMEGYLGRKHDLEGPN KKASNRSWNNLYCVLRNSEL TFYKDAKNLALGMPYHGEEP LALRHAICEIAANYKKKKHV FKLRLSNGSEWLFHGKDEEE MLSWLQGVSTAINESQSIRV KAQSLPLPSLSGPDASLGKK DKEKRFSFFPKKK in isoform 2. 1 PublicationAdd BLAST22

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32099.1. [P11277-2]
CCDS32100.1. [P11277-1]
PIRiA37064. SJHUB.
RefSeqiNP_000338.3. NM_000347.5. [P11277-1]
NP_001020029.1. NM_001024858.2. [P11277-2]
XP_005268080.1. XM_005268023.4. [P11277-2]
XP_016877101.1. XM_017021612.1. [P11277-2]
XP_016877103.1. XM_017021614.1. [P11277-1]
UniGeneiHs.417303.

Genome annotation databases

EnsembliENST00000389720; ENSP00000374370; ENSG00000070182. [P11277-3]
ENST00000389721; ENSP00000374371; ENSG00000070182. [P11277-1]
ENST00000389722; ENSP00000374372; ENSG00000070182. [P11277-2]
ENST00000556626; ENSP00000451752; ENSG00000070182. [P11277-2]
GeneIDi6710.
KEGGihsa:6710.
UCSCiuc001xhr.4. human. [P11277-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32099.1. [P11277-2]
CCDS32100.1. [P11277-1]
PIRiA37064. SJHUB.
RefSeqiNP_000338.3. NM_000347.5. [P11277-1]
NP_001020029.1. NM_001024858.2. [P11277-2]
XP_005268080.1. XM_005268023.4. [P11277-2]
XP_016877101.1. XM_017021612.1. [P11277-2]
XP_016877103.1. XM_017021614.1. [P11277-1]
UniGeneiHs.417303.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S35X-ray2.40A1063-1275[»]
3EDUX-ray2.10A1692-1907[»]
3F57X-ray2.90A/B1686-1907[»]
3KBTX-ray2.75A/B1583-1906[»]
3KBUX-ray2.75A/B1583-1906[»]
3LBXX-ray2.80B1902-2084[»]
ProteinModelPortaliP11277.
SMRiP11277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112588. 22 interactors.
DIPiDIP-1021N.
IntActiP11277. 8 interactors.
MINTiMINT-3007632.
STRINGi9606.ENSP00000374372.

PTM databases

iPTMnetiP11277.
PhosphoSitePlusiP11277.

Polymorphism and mutation databases

BioMutaiSPTB.
DMDMi215274269.

2D gel databases

SWISS-2DPAGEP11277.

Proteomic databases

EPDiP11277.
MaxQBiP11277.
PaxDbiP11277.
PeptideAtlasiP11277.
PRIDEiP11277.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389720; ENSP00000374370; ENSG00000070182. [P11277-3]
ENST00000389721; ENSP00000374371; ENSG00000070182. [P11277-1]
ENST00000389722; ENSP00000374372; ENSG00000070182. [P11277-2]
ENST00000556626; ENSP00000451752; ENSG00000070182. [P11277-2]
GeneIDi6710.
KEGGihsa:6710.
UCSCiuc001xhr.4. human. [P11277-1]

Organism-specific databases

CTDi6710.
DisGeNETi6710.
GeneCardsiSPTB.
HGNCiHGNC:11274. SPTB.
HPAiCAB015169.
CAB016232.
HPA003394.
HPA003398.
MalaCardsiSPTB.
MIMi182870. gene+phenotype.
616649. phenotype.
neXtProtiNX_P11277.
OpenTargetsiENSG00000070182.
Orphaneti288. Hereditary elliptocytosis.
822. Hereditary spherocytosis.
PharmGKBiPA36103.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0517. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000007281.
HOVERGENiHBG057912.
InParanoidiP11277.
KOiK06115.
OMAiGSEWLFH.
OrthoDBiEOG091G003V.
PhylomeDBiP11277.
TreeFamiTF313446.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000070182-MONOMER.
ReactomeiR-HSA-375165. NCAM signaling for neurite out-growth.
R-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

ChiTaRSiSPTB. human.
EvolutionaryTraceiP11277.
GeneWikiiSPTB.
GenomeRNAii6710.
PROiP11277.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000070182.
CleanExiHS_SPTB.
ExpressionAtlasiP11277. baseline and differential.
GenevisibleiP11277. HS.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00435. Spectrin. 17 hits.
[Graphical view]
PIRSFiPIRSF002297. Spectrin_beta_subunit. 1 hit.
SMARTiSM00033. CH. 2 hits.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPTB1_HUMAN
AccessioniPrimary (citable) accession number: P11277
Secondary accession number(s): Q15510, Q15519
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 184 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 14
    Human chromosome 14: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.