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P11277 (SPTB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spectrin beta chain, erythrocytic
Alternative name(s):
Beta-I spectrin
Gene names
Name:SPTB
Synonyms:SPTB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasmcytoskeleton. Cytoplasmcell 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 componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Elliptocytosis
Hereditary hemolytic anemia
   DomainRepeat
   LigandActin-binding
   Molecular functionActin capping
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Traceable author statement. Source: Reactome

hemopoiesis

Inferred from electronic annotation. Source: Ensembl

plasma membrane organization

Inferred from electronic annotation. Source: Ensembl

porphyrin-containing compound biosynthetic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentactin cytoskeleton

Traceable author statement PubMed 10950304. Source: BHF-UCL

cell surface

Inferred from direct assay PubMed 10867799. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

intrinsic component of the cytoplasmic side of the 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_functionactin binding

Traceable author statement Ref.1. Source: ProtInc

actin filament binding

Inferred from direct assay PubMed 16060676. Source: UniProtKB

ankyrin binding

Inferred from physical interaction PubMed 8159688. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 16060676. Source: UniProtKB

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SNAPINO952953EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 21372136Spectrin beta chain, erythrocytic
PRO_0000073459

Regions

Domain2 – 275274Actin-binding
Domain54 – 158105CH 1
Domain173 – 275103CH 2
Repeat276 – 384109Spectrin 1
Repeat385 – 498114Spectrin 2
Repeat499 – 607109Spectrin 3
Repeat608 – 713106Spectrin 4
Repeat714 – 818105Spectrin 5
Repeat819 – 924106Spectrin 6
Repeat925 – 1031107Spectrin 7
Repeat1032 – 1138107Spectrin 8
Repeat1139 – 1244106Spectrin 9
Repeat1245 – 1349105Spectrin 10
Repeat1350 – 1455106Spectrin 11
Repeat1456 – 155499Spectrin 12
Repeat1555 – 1660106Spectrin 13
Repeat1661 – 1767107Spectrin 14
Repeat1768 – 1873106Spectrin 15
Repeat1874 – 1979106Spectrin 16
Repeat1980 – 2085106Spectrin 17

Amino acid modifications

Modified residue21101Phosphothreonine Ref.11
Modified residue21141Phosphoserine Ref.11
Modified residue21171Phosphoserine Ref.11
Modified residue21231Phosphoserine Ref.11
Modified residue21251Phosphoserine Ref.11
Modified residue21281Phosphoserine Ref.11

Natural variations

Alternative sequence2074 – 213764LELKE…PSHPY → ASRGGRRDSRGGSSFPPCGH RENVPGQSLVSFV in isoform 3.
VSP_007242
Alternative sequence2116 – 213722VSLWS…PSHPY → GEEEGTWPQNLQQPPPPGQH KDGQKSTGDERPTTEPLFKV LDTPLSEGDEPATLPAPRDH GQSVQMEGYLGRKHDLEGPN KKASNRSWNNLYCVLRNSEL TFYKDAKNLALGMPYHGEEP LALRHAICEIAANYKKKKHV FKLRLSNGSEWLFHGKDEEE MLSWLQGVSTAINESQSIRV KAQSLPLPSLSGPDASLGKK DKEKRFSFFPKKK in isoform 2.
VSP_000719
Natural variant2021W → R in HS; Kissimmee. Ref.16
VAR_001352
Natural variant4391S → N. Ref.1
Corresponds to variant rs229587 [ dbSNP | Ensembl ].
VAR_001353
Natural variant5251E → K.
Corresponds to variant rs55752508 [ dbSNP | Ensembl ].
VAR_061084
Natural variant6131S → I.
Corresponds to variant rs3742601 [ dbSNP | Ensembl ].
VAR_038514
Natural variant11511N → D. Ref.1 Ref.4 Ref.6
Corresponds to variant rs77806 [ dbSNP | Ensembl ].
VAR_001354
Natural variant13741H → R. Ref.7
Corresponds to variant rs10132778 [ dbSNP | Ensembl ].
VAR_001355
Natural variant14031R → Q.
Corresponds to variant rs17180350 [ dbSNP | Ensembl ].
VAR_001356
Natural variant14081G → R.
Corresponds to variant rs17245552 [ dbSNP | Ensembl ].
VAR_038515
Natural variant20181A → G in EL3; Cagliary. Ref.15
VAR_001357
Natural variant20191S → P in EL3; Providence. Ref.17
VAR_001358
Natural variant20231A → V in EL3; Paris. Ref.18
VAR_001359
Natural variant20241W → R in EL3; Linguere. Ref.18
VAR_001360
Natural variant20251L → R in EL3; Buffalo.
VAR_001361
Natural variant20531A → P in EL3; Kayes. Ref.19
VAR_001362

Experimental info

Sequence conflict4031E → G in AAA60578. Ref.1
Sequence conflict4031E → G in AAA60579. Ref.1
Sequence conflict6121I → M in AAA60578. Ref.1
Sequence conflict6121I → M in AAA60579. Ref.1
Sequence conflict629 – 6313RKA → ART in AAA60578. Ref.1
Sequence conflict629 – 6313RKA → ART in AAA60579. Ref.1
Sequence conflict958 – 9592NY → TL in AAA60578. Ref.1
Sequence conflict958 – 9592NY → TL in AAA60579. Ref.1
Sequence conflict10311D → N in AAA60578. Ref.1
Sequence conflict10311D → N in AAA60579. Ref.1
Sequence conflict1844 – 18452EL → DV in AAA60578. Ref.1
Sequence conflict1844 – 18452EL → DV in AAA60579. Ref.1
Sequence conflict1844 – 18452EL → DV in AAA63259. Ref.3

Secondary structure

....................................... 2137
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 5.
Checksum: 311AE5CD53237610

FASTA2,137246,468
        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 

« Hide

Isoform 2 (Muscle-specific) [UniParc].

Checksum: 5C3709E99F70B8D0
Show »

FASTA2,328267,826
Isoform 3 [UniParc].

Checksum: E48305033176AE98
Show »

FASTA2,106242,802

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS32099.1. [P11277-2]
CCDS32100.1. [P11277-1]
PIRSJHUB. A37064.
RefSeqNP_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]
UniGeneHs.417303.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP11277.
SMRP11277. Positions 48-280, 299-2083.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112588. 10 interactions.
DIPDIP-1021N.
IntActP11277. 6 interactions.
MINTMINT-3007632.
STRING9606.ENSP00000374372.

PTM databases

PhosphoSiteP11277.

Polymorphism databases

DMDM215274269.

2D gel databases

SWISS-2DPAGEP11277.

Proteomic databases

MaxQBP11277.
PaxDbP11277.
PRIDEP11277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389720; ENSP00000374370; ENSG00000070182. [P11277-3]
ENST00000389721; ENSP00000374371; ENSG00000070182. [P11277-1]
ENST00000389722; ENSP00000374372; ENSG00000070182. [P11277-2]
ENST00000542895; ENSP00000443882; ENSG00000070182. [P11277-1]
ENST00000556626; ENSP00000451752; ENSG00000070182. [P11277-2]
GeneID6710.
KEGGhsa:6710.
UCSCuc001xhr.3. human. [P11277-2]
uc001xht.3. human. [P11277-1]

Organism-specific databases

CTD6710.
GeneCardsGC14M065213.
HGNCHGNC:11274. SPTB.
HPACAB015169.
HPA003394.
HPA003398.
MIM130600. phenotype.
182870. gene+phenotype.
neXtProtNX_P11277.
Orphanet98864. Common hereditary elliptocytosis.
98867. Hereditary pyropoikilocytosis.
822. Hereditary spherocytosis.
98866. Spherocytic elliptocytosis.
PharmGKBPA36103.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000007281.
HOVERGENHBG057912.
KOK06115.
OMAESFHRVH.
PhylomeDBP11277.
TreeFamTF313446.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressP11277.
BgeeP11277.
CleanExHS_SPTB.
GenevestigatorP11277.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF00435. Spectrin. 17 hits.
[Graphical view]
PIRSFPIRSF002297. Spectrin_beta_subunit. 1 hit.
SMARTSM00033. CH. 2 hits.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11277.
GeneWikiSPTB.
GenomeRNAi6710.
NextBio26166.
PROP11277.
SOURCESearch...

Entry information

Entry nameSPTB1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 160 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM