Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P11277

- SPTB1_HUMAN

UniProt

P11277 - SPTB1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Spectrin beta chain, erythrocytic

Gene

SPTB

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

Functioni

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

GO - Molecular functioni

  1. actin binding Source: ProtInc
  2. actin filament binding Source: UniProtKB
  3. ankyrin binding Source: BHF-UCL
  4. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. axon guidance Source: Reactome
  3. hemopoiesis Source: Ensembl
  4. plasma membrane organization Source: Ensembl
  5. porphyrin-containing compound biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain, erythrocytic
Alternative name(s):
Beta-I spectrin
Gene namesi
Name:SPTB
Synonyms:SPTB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:11274. SPTB.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: BHF-UCL
  2. cell surface Source: UniProtKB
  3. cytoplasm Source: HPA
  4. cytosol Source: Reactome
  5. intrinsic component of the cytoplasmic side of the plasma membrane Source: BHF-UCL
  6. protein complex Source: UniProtKB
  7. spectrin Source: ProtInc
  8. spectrin-associated cytoskeleton Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2018 – 20181A → G in EL3; Cagliary. 1 Publication
VAR_001357
Natural varianti2019 – 20191S → P in EL3; Providence. 1 Publication
VAR_001358
Natural varianti2023 – 20231A → V in EL3; Paris. 1 Publication
VAR_001359
Natural varianti2024 – 20241W → R in EL3; Linguere. 1 Publication
VAR_001360
Natural varianti2025 – 20251L → R in EL3; Buffalo.
VAR_001361
Natural varianti2053 – 20531A → P in EL3; Kayes. 1 Publication
VAR_001362
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.

Keywords - Diseasei

Disease mutation, Elliptocytosis, Hereditary hemolytic anemia

Organism-specific databases

MIMi130600. phenotype.
182870. gene+phenotype.
Orphaneti288. Hereditary elliptocytosis.
822. Hereditary spherocytosis.
PharmGKBiPA36103.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 21372136Spectrin beta chain, erythrocyticPRO_0000073459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2110 – 21101Phosphothreonine1 Publication
Modified residuei2114 – 21141Phosphoserine1 Publication
Modified residuei2117 – 21171Phosphoserine1 Publication
Modified residuei2123 – 21231Phosphoserine1 Publication
Modified residuei2125 – 21251Phosphoserine1 Publication
Modified residuei2128 – 21281Phosphoserine1 Publication

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

MaxQBiP11277.
PaxDbiP11277.
PRIDEiP11277.

2D gel databases

SWISS-2DPAGEP11277.

PTM databases

PhosphoSiteiP11277.

Expressioni

Gene expression databases

BgeeiP11277.
CleanExiHS_SPTB.
ExpressionAtlasiP11277. baseline and differential.
GenevestigatoriP11277.

Organism-specific databases

HPAiCAB015169.
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

Protein-protein interaction databases

BioGridi112588. 13 interactions.
DIPiDIP-1021N.
IntActiP11277. 6 interactions.
MINTiMINT-3007632.
STRINGi9606.ENSP00000374372.

Structurei

Secondary structure

1
2137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1065 – 108521Combined sources
Helixi1093 – 112836Combined sources
Helixi1134 – 119259Combined sources
Helixi1200 – 123637Combined sources
Helixi1242 – 127130Combined sources
Helixi1586 – 160520Combined sources
Helixi1616 – 165237Combined sources
Helixi1692 – 171322Combined sources
Helixi1722 – 175938Combined sources
Helixi1765 – 181854Combined sources
Helixi1838 – 186326Combined sources
Helixi1868 – 189124Combined sources
Helixi1902 – 192827Combined sources
Beta strandi1936 – 19383Combined sources
Helixi1941 – 197131Combined sources
Helixi1977 – 203357Combined sources
Helixi2041 – 206020Combined sources
Helixi2062 – 20698Combined sources
Helixi2073 – 208210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 50-280, 299-2083.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11277.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 275274Actin-bindingAdd
BLAST
Domaini54 – 158105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini173 – 275103CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati276 – 384109Spectrin 1Add
BLAST
Repeati385 – 498114Spectrin 2Add
BLAST
Repeati499 – 607109Spectrin 3Add
BLAST
Repeati608 – 713106Spectrin 4Add
BLAST
Repeati714 – 818105Spectrin 5Add
BLAST
Repeati819 – 924106Spectrin 6Add
BLAST
Repeati925 – 1031107Spectrin 7Add
BLAST
Repeati1032 – 1138107Spectrin 8Add
BLAST
Repeati1139 – 1244106Spectrin 9Add
BLAST
Repeati1245 – 1349105Spectrin 10Add
BLAST
Repeati1350 – 1455106Spectrin 11Add
BLAST
Repeati1456 – 155499Spectrin 12Add
BLAST
Repeati1555 – 1660106Spectrin 13Add
BLAST
Repeati1661 – 1767107Spectrin 14Add
BLAST
Repeati1768 – 1873106Spectrin 15Add
BLAST
Repeati1874 – 1979106Spectrin 16Add
BLAST
Repeati1980 – 2085106Spectrin 17Add
BLAST

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

eggNOGiCOG5069.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000007281.
HOVERGENiHBG057912.
InParanoidiP11277.
KOiK06115.
OMAiESFHRVH.
PhylomeDBiP11277.
TreeFamiTF313446.

Family and domain databases

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031E → G in AAA60578. (PubMed:2195026)Curated
Sequence conflicti403 – 4031E → G in AAA60579. (PubMed:2195026)Curated
Sequence conflicti612 – 6121I → M in AAA60578. (PubMed:2195026)Curated
Sequence conflicti612 – 6121I → M in AAA60579. (PubMed:2195026)Curated
Sequence conflicti629 – 6313RKA → ART in AAA60578. (PubMed:2195026)Curated
Sequence conflicti629 – 6313RKA → ART in AAA60579. (PubMed:2195026)Curated
Sequence conflicti958 – 9592NY → TL in AAA60578. (PubMed:2195026)Curated
Sequence conflicti958 – 9592NY → TL in AAA60579. (PubMed:2195026)Curated
Sequence conflicti1031 – 10311D → N in AAA60578. (PubMed:2195026)Curated
Sequence conflicti1031 – 10311D → N in AAA60579. (PubMed:2195026)Curated
Sequence conflicti1844 – 18452EL → DV in AAA60578. (PubMed:2195026)Curated
Sequence conflicti1844 – 18452EL → DV in AAA60579. (PubMed:2195026)Curated
Sequence conflicti1844 – 18452EL → DV in AAA63259. (PubMed:2056132)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti202 – 2021W → R in HS; Kissimmee. 1 Publication
VAR_001352
Natural varianti439 – 4391S → N.1 Publication
Corresponds to variant rs229587 [ dbSNP | Ensembl ].
VAR_001353
Natural varianti525 – 5251E → K.
Corresponds to variant rs55752508 [ dbSNP | Ensembl ].
VAR_061084
Natural varianti613 – 6131S → I.
Corresponds to variant rs3742601 [ dbSNP | Ensembl ].
VAR_038514
Natural varianti1151 – 11511N → D.3 Publications
Corresponds to variant rs77806 [ dbSNP | Ensembl ].
VAR_001354
Natural varianti1374 – 13741H → R.1 Publication
Corresponds to variant rs10132778 [ dbSNP | Ensembl ].
VAR_001355
Natural varianti1403 – 14031R → Q.
Corresponds to variant rs17180350 [ dbSNP | Ensembl ].
VAR_001356
Natural varianti1408 – 14081G → R.
Corresponds to variant rs17245552 [ dbSNP | Ensembl ].
VAR_038515
Natural varianti2018 – 20181A → G in EL3; Cagliary. 1 Publication
VAR_001357
Natural varianti2019 – 20191S → P in EL3; Providence. 1 Publication
VAR_001358
Natural varianti2023 – 20231A → V in EL3; Paris. 1 Publication
VAR_001359
Natural varianti2024 – 20241W → R in EL3; Linguere. 1 Publication
VAR_001360
Natural varianti2025 – 20251L → R in EL3; Buffalo.
VAR_001361
Natural varianti2053 – 20531A → P in EL3; Kayes. 1 Publication
VAR_001362

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2074 – 213764LELKE…PSHPY → ASRGGRRDSRGGSSFPPCGH RENVPGQSLVSFV in isoform 3. 1 PublicationVSP_007242Add
BLAST
Alternative sequencei2116 – 213722VSLWS…PSHPY → GEEEGTWPQNLQQPPPPGQH KDGQKSTGDERPTTEPLFKV LDTPLSEGDEPATLPAPRDH GQSVQMEGYLGRKHDLEGPN KKASNRSWNNLYCVLRNSEL TFYKDAKNLALGMPYHGEEP LALRHAICEIAANYKKKKHV FKLRLSNGSEWLFHGKDEEE MLSWLQGVSTAINESQSIRV KAQSLPLPSLSGPDASLGKK DKEKRFSFFPKKK in isoform 2. 1 PublicationVSP_000719Add
BLAST

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_005268023.2. [P11277-2]
XP_006720304.1. XM_006720241.1. [P11277-2]
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.3. human. [P11277-2]
uc001xht.3. human. [P11277-1]

Polymorphism databases

DMDMi215274269.

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 .
CCDSi CCDS32099.1. [P11277-2 ]
CCDS32100.1. [P11277-1 ]
PIRi A37064. SJHUB.
RefSeqi NP_000338.3. NM_000347.5. [P11277-1 ]
NP_001020029.1. NM_001024858.2. [P11277-2 ]
XP_005268080.1. XM_005268023.2. [P11277-2 ]
XP_006720304.1. XM_006720241.1. [P11277-2 ]
UniGenei Hs.417303.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1S35 X-ray 2.40 A 1063-1275 [» ]
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 [» ]
ProteinModelPortali P11277.
SMRi P11277. Positions 50-280, 299-2083.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112588. 13 interactions.
DIPi DIP-1021N.
IntActi P11277. 6 interactions.
MINTi MINT-3007632.
STRINGi 9606.ENSP00000374372.

PTM databases

PhosphoSitei P11277.

Polymorphism databases

DMDMi 215274269.

2D gel databases

SWISS-2DPAGE P11277.

Proteomic databases

MaxQBi P11277.
PaxDbi P11277.
PRIDEi P11277.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389720 ; ENSP00000374370 ; ENSG00000070182 . [P11277-3 ]
ENST00000389721 ; ENSP00000374371 ; ENSG00000070182 . [P11277-1 ]
ENST00000389722 ; ENSP00000374372 ; ENSG00000070182 . [P11277-2 ]
ENST00000556626 ; ENSP00000451752 ; ENSG00000070182 . [P11277-2 ]
GeneIDi 6710.
KEGGi hsa:6710.
UCSCi uc001xhr.3. human. [P11277-2 ]
uc001xht.3. human. [P11277-1 ]

Organism-specific databases

CTDi 6710.
GeneCardsi GC14M065213.
HGNCi HGNC:11274. SPTB.
HPAi CAB015169.
HPA003394.
HPA003398.
MIMi 130600. phenotype.
182870. gene+phenotype.
neXtProti NX_P11277.
Orphaneti 288. Hereditary elliptocytosis.
822. Hereditary spherocytosis.
PharmGKBi PA36103.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000118813.
HOGENOMi HOG000007281.
HOVERGENi HBG057912.
InParanoidi P11277.
KOi K06115.
OMAi ESFHRVH.
PhylomeDBi P11277.
TreeFami TF313446.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi SPTB. human.
EvolutionaryTracei P11277.
GeneWikii SPTB.
GenomeRNAii 6710.
NextBioi 26166.
PROi P11277.
SOURCEi Search...

Gene expression databases

Bgeei P11277.
CleanExi HS_SPTB.
ExpressionAtlasi P11277. baseline and differential.
Genevestigatori P11277.

Family and domain databases

Gene3Di 1.10.418.10. 2 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view ]
Pfami PF00307. CH. 2 hits.
PF00435. Spectrin. 17 hits.
[Graphical view ]
PIRSFi PIRSF002297. Spectrin_beta_subunit. 1 hit.
SMARTi SM00033. CH. 2 hits.
SM00150. SPEC. 17 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

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 26, 2014
This is version 164 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

External Data

Dasty 3