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Protein

Spectrin beta chain, erythrocytic

Gene

Sptb

Organism
Mus musculus (Mouse)
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: MGI
  • actin filament binding Source: MGI
  • ankyrin binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • hemopoiesis Source: MGI
  • plasma membrane organization Source: MGI
  • porphyrin-containing compound biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain, erythrocytic
Alternative name(s):
Beta-I spectrin
Gene namesi
Name:Sptb
Synonyms:Spnb-1, Spnb1, Sptb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:98387. Sptb.

Subcellular locationi

GO - Cellular componenti

  • cortical cytoskeleton Source: MGI
  • cytoplasm Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: MGI
  • protein complex Source: MGI
  • spectrin Source: InterPro
  • spectrin-associated cytoskeleton Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000734602 – 2128Spectrin beta chain, erythrocyticAdd BLAST2127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36PhosphoserineCombined sources1
Modified residuei104PhosphothreonineBy similarity1
Modified residuei1289PhosphoserineCombined sources1
Modified residuei2034PhosphoserineBy similarity1
Modified residuei2064PhosphothreonineBy similarity1
Modified residuei2072PhosphothreonineCombined sources1
Modified residuei2101PhosphothreonineBy similarity1
Modified residuei2105PhosphoserineBy similarity1
Modified residuei2108PhosphoserineBy similarity1
Modified residuei2114PhosphoserineBy similarity1
Modified residuei2116PhosphoserineBy similarity1
Modified residuei2119PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15508.
PaxDbiP15508.
PeptideAtlasiP15508.
PRIDEiP15508.

PTM databases

iPTMnetiP15508.
PhosphoSitePlusiP15508.

Expressioni

Gene expression databases

CleanExiMM_SPNB1.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: MGI
  • ankyrin binding Source: MGI
  • protein heterodimerization activity Source: MGI

Protein-protein interaction databases

IntActiP15508. 3 interactors.
MINTiMINT-4996478.
STRINGi10090.ENSMUSP00000021458.

Structurei

3D structure databases

ProteinModelPortaliP15508.
SMRiP15508.
ModBaseiSearch...
MobiDBiSearch...

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 – 490Spectrin 2Add BLAST106
Repeati491 – 599Spectrin 3Add BLAST109
Repeati600 – 705Spectrin 4Add BLAST106
Repeati706 – 810Spectrin 5Add BLAST105
Repeati811 – 916Spectrin 6Add BLAST106
Repeati917 – 1023Spectrin 7Add BLAST107
Repeati1024 – 1130Spectrin 8Add BLAST107
Repeati1131 – 1236Spectrin 9Add BLAST106
Repeati1237 – 1341Spectrin 10Add BLAST105
Repeati1342 – 1447Spectrin 11Add BLAST106
Repeati1448 – 1546Spectrin 12Add BLAST99
Repeati1547 – 1652Spectrin 13Add BLAST106
Repeati1653 – 1759Spectrin 14Add BLAST107
Repeati1760 – 1864Spectrin 15Add BLAST105
Repeati1865 – 1970Spectrin 16Add BLAST106
Repeati1971 – 2073Spectrin 17Add BLAST103

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.
HOVERGENiHBG057912.
InParanoidiP15508.

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]

Sequencei

Sequence statusi: Complete.

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

P15508-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSATEFENV GNQPPFSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD
60 70 80 90 100
EREVVQKKTF TKWVNSHLAR VSCRISDLYK DLRDGRMLIK LLEVLSGEML
110 120 130 140 150
PRPTKGKMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI
160 170 180 190 200
WTIILRFQIQ DIVVQTQEGR EQRSAKDALL LWCQMKTAGY PHVNVTNFTS
210 220 230 240 250
SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFDV AERQLGIIPL
260 270 280 290 300
LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET
310 320 330 340 350
EKMIEKYSGL ASDLLTWIEQ TISVLNSRKF ANSLSGVQQQ LQAFSTYRTV
360 370 380 390 400
EKPPKFQEKG NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE
410 420 430 440 450
EAEYQRELAL RSELIRQEFD RKAAMRETWL NENQRLVTQD NFGYDLAAVE
460 470 480 490 500
AAKKKHEAIE TDTAAYEERV KALEDLAQEL EKENYHDQKR IIARKDNILR
510 520 530 540 550
LWSYLQELLR SRRQRLEATL ALQKLFQDML HSIDWMDEIK AHILSAEFGK
560 570 580 590 600
HLLEVEDLLQ KHKLMEADIA IQGDKVKAIT AATLQFAEGK GYQPCDPQVI
610 620 630 640 650
QDRVSHLEQC FSELSNMAAG RKAQLEQSKR LWKFFWEMDE AESWIKEKEQ
660 670 680 690 700
IYSSLDYGKD LTSVLILQRK HKAFEDELRG LDAHLKQIFQ EADDMVAQKQ
710 720 730 740 750
FGHPQIETRV KEVSAQWDHL KELAAFRKKD LQDAENFFQF QGDADDLKAW
760 770 780 790 800
LQDAHRLLSG EDVGQDEGAT RALGKKHKEF LEELEESRGV MEHLEHQAQG
810 820 830 840 850
FPEEFRDSPD VTNRLQALRK LYQQVLTQAE LRGHKLQEAL DLYTVFGESD
860 870 880 890 900
ACELWMTEKG KWLDQMDIPN TLEDLEVVQH RFDILDQEMK TLMAQIDGVN
910 920 930 940 950
LAANNLVESG HPRSGEVKQY QDRLNKRWQA FQAVVSEQRE AVDSALRVNN
960 970 980 990 1000
YCVDCEETSK WIMDKTKVVE STKDLGQDLA GVIAIQRKLS GLERDVLAIR
1010 1020 1030 1040 1050
DRVSALERES QYLMESHPEQ KEDIGQRQAD VEKLWKGLQD ALQGQELSLG
1060 1070 1080 1090 1100
EASKLQAFLQ DLDDFKAWLS MAQKAVASED MPESLPEAEQ LLQQHAAIKE
1110 1120 1130 1140 1150
EIDAHRDDYH RVKASGEKVI EGQTDPDYQL LGQRLEGLDT DWDALRRMWE
1160 1170 1180 1190 1200
SRGNTLTQCL GFQEFQKDAK QAEAILSNQE YTLAHLEPPD SLAAAEAGIR
1210 1220 1230 1240 1250
KFEDFLVSME NNRDKILSPV DSGNKLVAEG NLYSNKIMEK VQLIEDRHKK
1260 1270 1280 1290 1300
NNEKAQEATV LLKDNLELQN FLQNCKELTL WINDKLLTSP DVSYDEARNL
1310 1320 1330 1340 1350
HNKWMKHQAF MAELASHQGW LENIDAEGRQ LMAEKPQFKD VVSERLEALH
1360 1370 1380 1390 1400
KLWEELQSTA KAKAEQLSAA RSSDLRLQTH ADLNKWIGAM EDQLRSDDLG
1410 1420 1430 1440 1450
KDLTTVNRML AKLKRVEEQV NLRKEELEEL FADAPSLGAE AGDTDMSIEK
1460 1470 1480 1490 1500
RFLDLLEPLG RRKKQLELSK AKLQISRDLE DETLWVEERL PLAQSADYGT
1510 1520 1530 1540 1550
NLQTVQLFMK KNQTLQNEIL GHAPRVEDVL RRGQELVKAA EIDCQDIEER
1560 1570 1580 1590 1600
LGHLQSSWDT LREAAAGRLQ RLRDAHEAQQ YYLDAGEAEA WISEQELYVF
1610 1620 1630 1640 1650
SDEPPKDEEG AIVMLKRHLR QQRTVEEYGR NIKQLAGRAQ SLLSAGHPEG
1660 1670 1680 1690 1700
EQIIRLQGQV DKQYAGLKDM AEERRRRLEN MYHLFQLKRE ADDLEQWITE
1710 1720 1730 1740 1750
KEMVASSQEM GQDFDHVTML RDKFRDFARE TGAIGQERVD NVTIIERLID
1760 1770 1780 1790 1800
AGHSEAATIA EWKDGLNDMW ADLLELIDTR MQLLAASYDL HRYFYTGTEI
1810 1820 1830 1840 1850
LGLIDEKHRE LPEDVGLDAS TAESFHRVHT AFERELHLLG VQVQQFQDVA
1860 1870 1880 1890 1900
TRLQTAYAGE KADAIQSKEQ EVSAAWQALL DACAGRRAQL VDTADKFRFF
1910 1920 1930 1940 1950
SMVRDLLSWM ESIIRQIETQ ERPRDVSSVE LLLKYHQGIK AEINTRAKNF
1960 1970 1980 1990 2000
STCLELGESL LQRQHQASDE IREKLQQVIS RRQEMNDKWE ARSDRLHMLL
2010 2020 2030 2040 2050
EVCQFSRDAS VAEAWLIAQE PYLASRDFGH TVDSVEKLIK RHEAFEKSTA
2060 2070 2080 2090 2100
SWAERFAALE KPTTLELKER QTPERPTEEP GPQEEEGETA GEAPQVHHAA
2110 2120
TERTSPVSFM SRLSSSWESL LPEPAHPF
Length:2,128
Mass (Da):245,250
Last modified:January 23, 2007 - v4
Checksum:i10E576111106DFE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S66283 mRNA. Translation: AAB28600.1.
M18641 mRNA. Translation: AAA40126.1.
PIRiA45929.
UniGeneiMm.32881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S66283 mRNA. Translation: AAB28600.1.
M18641 mRNA. Translation: AAA40126.1.
PIRiA45929.
UniGeneiMm.32881.

3D structure databases

ProteinModelPortaliP15508.
SMRiP15508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP15508. 3 interactors.
MINTiMINT-4996478.
STRINGi10090.ENSMUSP00000021458.

PTM databases

iPTMnetiP15508.
PhosphoSitePlusiP15508.

Proteomic databases

MaxQBiP15508.
PaxDbiP15508.
PeptideAtlasiP15508.
PRIDEiP15508.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:98387. Sptb.

Phylogenomic databases

eggNOGiKOG0517. Eukaryota.
COG5069. LUCA.
HOVERGENiHBG057912.
InParanoidiP15508.

Miscellaneous databases

PROiP15508.
SOURCEiSearch...

Gene expression databases

CleanExiMM_SPNB1.

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_MOUSE
AccessioniPrimary (citable) accession number: P15508
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.