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Protein

Spectrin beta chain, non-erythrocytic 1

Gene

SPTBN1

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

Functioni

Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane.

GO - Molecular functioni

  • actin binding Source: ProtInc
  • ankyrin binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • GTPase binding Source: UniProtKB
  • phospholipid binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • structural constituent of cytoskeleton Source: BHF-UCL

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • axon guidance Source: Reactome
  • common-partner SMAD protein phosphorylation Source: Ensembl
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • Golgi to plasma membrane protein transport Source: BHF-UCL
  • MAPK cascade Source: Reactome
  • membrane assembly Source: BHF-UCL
  • mitotic cytokinesis Source: BHF-UCL
  • plasma membrane organization Source: BHF-UCL
  • positive regulation of interleukin-2 secretion Source: UniProtKB
  • positive regulation of protein localization to plasma membrane Source: UniProtKB
  • protein targeting to plasma membrane Source: BHF-UCL
  • regulation of protein localization to plasma membrane Source: UniProtKB
  • SMAD protein import into nucleus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115306-MONOMER.
ReactomeiR-HSA-373753. Nephrin interactions.
R-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.
SignaLinkiQ01082.
SIGNORiQ01082.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain, non-erythrocytic 1
Alternative name(s):
Beta-II spectrin
Fodrin beta chain
Spectrin, non-erythroid beta chain 1
Gene namesi
Name:SPTBN1
Synonyms:SPTB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11275. SPTBN1.

Subcellular locationi

Isoform 2 :

GO - Cellular componenti

  • axolemma Source: BHF-UCL
  • cell-cell adherens junction Source: BHF-UCL
  • cuticular plate Source: Ensembl
  • cytoplasm Source: HGNC
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • M band Source: UniProtKB-SubCell
  • nucleolus Source: HGNC
  • postsynaptic density Source: Ensembl
  • protein complex Source: Ensembl
  • spectrin Source: ProtInc
  • spectrin-associated cytoskeleton Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi6711.
OpenTargetsiENSG00000115306.
PharmGKBiPA36104.

Polymorphism and mutation databases

BioMutaiSPTBN1.
DMDMi116242799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000734612 – 2364Spectrin beta chain, non-erythrocytic 1Add BLAST2363

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei36PhosphoserineBy similarity1
Modified residuei90N6-acetyllysineCombined sources1
Modified residuei228PhosphoserineBy similarity1
Modified residuei817PhosphoserineCombined sources1
Modified residuei825PhosphoserineCombined sources1
Modified residuei903PhosphoserineBy similarity1
Modified residuei1057PhosphoserineCombined sources1
Modified residuei1076PhosphoserineBy similarity1
Modified residuei1079PhosphoserineBy similarity1
Modified residuei1237PhosphoserineCombined sources1
Modified residuei1388PhosphoserineCombined sources1
Modified residuei1447PhosphoserineCombined sources1
Modified residuei1557PhosphoserineCombined sources1
Modified residuei1805PhosphotyrosineBy similarity1
Modified residuei1815N6-acetyllysineCombined sources1
Modified residuei1913N6-acetyllysineCombined sources1
Modified residuei1989N6-acetyllysineCombined sources1
Modified residuei2102PhosphoserineCombined sources1
Modified residuei2128PhosphoserineCombined sources1
Modified residuei2138PhosphoserineCombined sources1
Modified residuei2147PhosphothreonineBy similarity1
Modified residuei2148PhosphoserineBy similarity1
Modified residuei2159PhosphothreonineBy similarity1
Modified residuei2160PhosphoserineCombined sources1
Modified residuei2161PhosphoserineCombined sources1
Modified residuei2164PhosphoserineCombined sources1
Modified residuei2165PhosphoserineCombined sources1
Modified residuei2169PhosphoserineCombined sources1
Modified residuei2171PhosphothreonineBy similarity1
Modified residuei2172PhosphoserineCombined sources1
Modified residuei2184PhosphoserineBy similarity1
Modified residuei2187PhosphothreonineCombined sources1
Modified residuei2195PhosphothreonineBy similarity1
Modified residuei2314PhosphoserineCombined sources1
Modified residuei2319PhosphoserineCombined sources1
Modified residuei2320PhosphothreonineCombined sources1
Glycosylationi2324O-linked (GlcNAc)By similarity1
Modified residuei2328PhosphothreonineCombined sources1
Modified residuei2340PhosphoserineCombined sources1
Modified residuei2341PhosphoserineCombined sources1
Isoform 2 (identifier: Q01082-3)
Modified residuei14PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ01082.
MaxQBiQ01082.
PaxDbiQ01082.
PeptideAtlasiQ01082.
PRIDEiQ01082.

PTM databases

iPTMnetiQ01082.
PhosphoSitePlusiQ01082.
SwissPalmiQ01082.

Expressioni

Tissue specificityi

Isoform 2 is present in brain, lung and kidney (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000115306.
CleanExiHS_SPTBN1.
ExpressionAtlasiQ01082. baseline and differential.
GenevisibleiQ01082. HS.

Organism-specific databases

HPAiHPA012685.
HPA013149.

Interactioni

Subunit structurei

Interacts with CAMSAP1 (PubMed:24117850). Interacts with ANK2 (PubMed:15262991). Interacts with CPNE4 (via VWFA domain) (By similarity). Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers (By similarity). Isoform Short cannot bind to the axonal protein fodaxin.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DISC1Q9NRI53EBI-351561,EBI-529989
SPTA1P025493EBI-351561,EBI-375617
SPTAN1Q138137EBI-351561,EBI-351450

GO - Molecular functioni

  • actin binding Source: ProtInc
  • ankyrin binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112589. 124 interactors.
DIPiDIP-33182N.
IntActiQ01082. 84 interactors.
MINTiMINT-1136298.
STRINGi9606.ENSP00000349259.

Structurei

Secondary structure

12364
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi174 – 186Combined sources13
Turni187 – 189Combined sources3
Beta strandi196 – 199Combined sources4
Helixi200 – 202Combined sources3
Helixi206 – 215Combined sources10
Helixi217 – 219Combined sources3
Helixi222 – 224Combined sources3
Helixi230 – 245Combined sources16
Helixi253 – 256Combined sources4
Beta strandi257 – 260Combined sources4
Helixi263 – 277Combined sources15
Helixi1697 – 1721Combined sources25
Helixi1730 – 1767Combined sources38
Helixi1773 – 1826Combined sources54
Helixi1836 – 1852Combined sources17
Helixi1854 – 1873Combined sources20
Helixi1877 – 1935Combined sources59
Helixi1943 – 1962Combined sources20
Helixi1964 – 1979Combined sources16
Helixi1985 – 2014Combined sources30

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AA2X-ray2.00A173-280[»]
1BKRX-ray1.10A172-280[»]
3EDVX-ray1.95A/B1697-2015[»]
ProteinModelPortaliQ01082.
SMRiQ01082.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01082.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 275Actin-bindingAdd BLAST275
Domaini54 – 158CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini173 – 275CH 2PROSITE-ProRule annotationAdd BLAST103
Repeati303 – 411Spectrin 1Add BLAST109
Repeati423 – 525Spectrin 2Add BLAST103
Repeati530 – 636Spectrin 3Add BLAST107
Repeati639 – 742Spectrin 4Add BLAST104
Repeati745 – 847Spectrin 5Add BLAST103
Repeati851 – 952Spectrin 6Add BLAST102
Repeati957 – 1060Spectrin 7Add BLAST104
Repeati1063 – 1166Spectrin 8Add BLAST104
Repeati1169 – 1257Spectrin 9Add BLAST89
Repeati1276 – 1376Spectrin 10Add BLAST101
Repeati1381 – 1482Spectrin 11Add BLAST102
Repeati1486 – 1590Spectrin 12Add BLAST105
Repeati1592 – 1696Spectrin 13Add BLAST105
Repeati1698 – 1801Spectrin 14Add BLAST104
Repeati1805 – 1907Spectrin 15Add BLAST103
Repeati1914 – 2014Spectrin 16Add BLAST101
Repeati2018 – 2097Spectrin 17Add BLAST80
Domaini2197 – 2307PHPROSITE-ProRule annotationAdd BLAST111

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1563 – 2093Interaction with ANK21 PublicationAdd BLAST531
Regioni2149 – 2177Mediates interaction with CAMSAP11 PublicationAdd BLAST29

Sequence similaritiesi

Belongs to the spectrin family.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 17 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOVERGENiHBG057912.
InParanoidiQ01082.
KOiK06115.
PhylomeDBiQ01082.
TreeFamiTF313446.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011993. PH_dom-like.
IPR001605. PH_dom-spectrin-type.
IPR001849. PH_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.
PRINTSiPR00683. SPECTRINPH.
SMARTiSM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[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 Long (identifier: Q01082-1) [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
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD
60 70 80 90 100
EREAVQKKTF TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL
110 120 130 140 150
PKPTKGRMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI
160 170 180 190 200
WTIILRFQIQ DISVETEDNK EKKSAKDALL LWCQMKTAGY PNVNIHNFTT
210 220 230 240 250
SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL AEQHLGLTKL
260 270 280 290 300
LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
310 320 330 340 350
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV
360 370 380 390 400
EKPPKFTEKG NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE
410 420 430 440 450
KAEHERELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVSQDNF
460 470 480 490 500
GFDLPAVEAA TKKHEAIETD IAAYEERVQA VVAVARELEA ENYHDIKRIT
510 520 530 540 550
ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI MDWMDEMKVL
560 570 580 590 600
VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG
610 620 630 640 650
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE
660 670 680 690 700
EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE
710 720 730 740 750
GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ
760 770 780 790 800
ADADDIDAWM LDILKIVSSS DVGHDEYSTQ SLVKKHKDVA EEIANYRPTL
810 820 830 840 850
DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL RKQALQDTLA
860 870 880 890 900
LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
910 920 930 940 950
QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA
960 970 980 990 1000
LLSALSIQNY HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG
1010 1020 1030 1040 1050
MERDLVAIEA KLSDLQKEAE KLESEHPDQA QAILSRLAEI SDVWEEMKTT
1060 1070 1080 1090 1100
LKNREASLGE ASKLQQFLRD LDDFQSWLSR TQTAIASEDM PNTLTEAEKL
1110 1120 1130 1140 1150
LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL RQRLQALDTG
1160 1170 1180 1190 1200
WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
1210 1220 1230 1240 1250
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV
1260 1270 1280 1290 1300
DSIDDRHRKN RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD
1310 1320 1330 1340 1350
MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV
1360 1370 1380 1390 1400
VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE
1410 1420 1430 1440 1450
SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG
1460 1470 1480 1490 1500
KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW
1510 1520 1530 1540 1550
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN
1560 1570 1580 1590 1600
IVTDSSSLSA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD
1610 1620 1630 1640 1650
AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ
1660 1670 1680 1690 1700
LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL
1710 1720 1730 1740 1750
FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI
1760 1770 1780 1790 1800
GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
1810 1820 1830 1840 1850
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE
1860 1870 1880 1890 1900
HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC
1910 1920 1930 1940 1950
ESRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM
1960 1970 1980 1990 2000
NNHQGIKAEI DARNDSFTTC IELGKSLLAR KHYASEEIKE KLLQLTEKRK
2010 2020 2030 2040 2050
EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD
2060 2070 2080 2090 2100
EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
2110 2120 2130 2140 2150
PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM
2160 2170 2180 2190 2200
VNGATEQRTS SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM
2210 2220 2230 2240 2250
EGFLNRKHEW EAHNKKASSR SWHNVYCVIN NQEMGFYKDA KTAASGIPYH
2260 2270 2280 2290 2300
SEVPVSLKEA VCEVALDYKK KKHVFKLRLN DGNEYLFQAK DDEEMNTWIQ
2310 2320 2330 2340 2350
AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES SPGKREKDKE
2360
KDKEKRFSLF GKKK
Length:2,364
Mass (Da):274,609
Last modified:October 17, 2006 - v2
Checksum:i1770C3B0EB07B892
GO
Isoform Short (identifier: Q01082-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2141-2168: MAETVDTSEMVNGATEQRTSSKESSPIP → VSYRSQTYQNYKNFNSRRTASDQPWSGL
     2169-2364: Missing.

Show »
Length:2,168
Mass (Da):253,091
Checksum:i34F9C77E47199043
GO
Isoform 2 (identifier: Q01082-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MTTTVATDYD...FERSRIKALA → MELQRTSSIS...QLEGRFKQLQ
     2141-2225: MAETVDTSEM...KASSRSWHNV → VSYRSQTYQNYKNFNSRRTASDQPWSGL
     2226-2364: Missing.

Show »
Length:2,155
Mass (Da):251,397
Checksum:i2CA864D7AAC0182C
GO

Sequence cautioni

The sequence BAD92985 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti583R → W in BAD92985 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0326411411D → H.2 PublicationsCorresponds to variant rs1052790dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0260541 – 49MTTTV…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2. 2 PublicationsAdd BLAST49
Alternative sequenceiVSP_0260552141 – 2225MAETV…SWHNV → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform 2. 2 PublicationsAdd BLAST85
Alternative sequenceiVSP_0007202141 – 2168MAETV…SSPIP → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform Short. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_0007212169 – 2364Missing in isoform Short. 1 PublicationAdd BLAST196
Alternative sequenceiVSP_0260562226 – 2364Missing in isoform 2. 2 PublicationsAdd BLAST139

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96803 mRNA. Translation: AAA60580.1.
AF327441 mRNA. Translation: AAO15362.1.
AB209748 mRNA. Translation: BAD92985.1. Different initiation.
AC093110 Genomic DNA. Translation: AAY24229.1.
AC092839 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00147.1.
BC137282 mRNA. Translation: AAI37283.1.
BC137283 mRNA. Translation: AAI37284.1.
S65762 mRNA. Translation: AAB28324.1.
AJ005694 mRNA. Translation: CAA06678.1.
AJ238723 Genomic DNA. Translation: CAB91088.1.
CCDSiCCDS33198.1. [Q01082-1]
CCDS33199.1. [Q01082-3]
PIRiA44159.
A47213.
RefSeqiNP_003119.2. NM_003128.2. [Q01082-1]
NP_842565.2. NM_178313.2. [Q01082-3]
XP_005264574.1. XM_005264517.2. [Q01082-1]
XP_006712150.1. XM_006712087.2. [Q01082-1]
XP_016860268.1. XM_017004779.1. [Q01082-1]
XP_016860269.1. XM_017004780.1. [Q01082-1]
XP_016860270.1. XM_017004781.1. [Q01082-1]
UniGeneiHs.503178.
Hs.705692.

Genome annotation databases

EnsembliENST00000333896; ENSP00000334156; ENSG00000115306. [Q01082-3]
ENST00000356805; ENSP00000349259; ENSG00000115306. [Q01082-1]
GeneIDi6711.
KEGGihsa:6711.
UCSCiuc002rxu.4. human. [Q01082-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96803 mRNA. Translation: AAA60580.1.
AF327441 mRNA. Translation: AAO15362.1.
AB209748 mRNA. Translation: BAD92985.1. Different initiation.
AC093110 Genomic DNA. Translation: AAY24229.1.
AC092839 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00147.1.
BC137282 mRNA. Translation: AAI37283.1.
BC137283 mRNA. Translation: AAI37284.1.
S65762 mRNA. Translation: AAB28324.1.
AJ005694 mRNA. Translation: CAA06678.1.
AJ238723 Genomic DNA. Translation: CAB91088.1.
CCDSiCCDS33198.1. [Q01082-1]
CCDS33199.1. [Q01082-3]
PIRiA44159.
A47213.
RefSeqiNP_003119.2. NM_003128.2. [Q01082-1]
NP_842565.2. NM_178313.2. [Q01082-3]
XP_005264574.1. XM_005264517.2. [Q01082-1]
XP_006712150.1. XM_006712087.2. [Q01082-1]
XP_016860268.1. XM_017004779.1. [Q01082-1]
XP_016860269.1. XM_017004780.1. [Q01082-1]
XP_016860270.1. XM_017004781.1. [Q01082-1]
UniGeneiHs.503178.
Hs.705692.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AA2X-ray2.00A173-280[»]
1BKRX-ray1.10A172-280[»]
3EDVX-ray1.95A/B1697-2015[»]
ProteinModelPortaliQ01082.
SMRiQ01082.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112589. 124 interactors.
DIPiDIP-33182N.
IntActiQ01082. 84 interactors.
MINTiMINT-1136298.
STRINGi9606.ENSP00000349259.

PTM databases

iPTMnetiQ01082.
PhosphoSitePlusiQ01082.
SwissPalmiQ01082.

Polymorphism and mutation databases

BioMutaiSPTBN1.
DMDMi116242799.

Proteomic databases

EPDiQ01082.
MaxQBiQ01082.
PaxDbiQ01082.
PeptideAtlasiQ01082.
PRIDEiQ01082.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333896; ENSP00000334156; ENSG00000115306. [Q01082-3]
ENST00000356805; ENSP00000349259; ENSG00000115306. [Q01082-1]
GeneIDi6711.
KEGGihsa:6711.
UCSCiuc002rxu.4. human. [Q01082-1]

Organism-specific databases

CTDi6711.
DisGeNETi6711.
GeneCardsiSPTBN1.
H-InvDBHIX0002055.
HGNCiHGNC:11275. SPTBN1.
HPAiHPA012685.
HPA013149.
MIMi182790. gene.
neXtProtiNX_Q01082.
OpenTargetsiENSG00000115306.
PharmGKBiPA36104.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOVERGENiHBG057912.
InParanoidiQ01082.
KOiK06115.
PhylomeDBiQ01082.
TreeFamiTF313446.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115306-MONOMER.
ReactomeiR-HSA-373753. Nephrin interactions.
R-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.
SignaLinkiQ01082.
SIGNORiQ01082.

Miscellaneous databases

ChiTaRSiSPTBN1. human.
EvolutionaryTraceiQ01082.
GeneWikiiSPTBN1.
GenomeRNAii6711.
PROiQ01082.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000115306.
CleanExiHS_SPTBN1.
ExpressionAtlasiQ01082. baseline and differential.
GenevisibleiQ01082. HS.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011993. PH_dom-like.
IPR001605. PH_dom-spectrin-type.
IPR001849. PH_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.
PRINTSiPR00683. SPECTRINPH.
SMARTiSM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPTB2_HUMAN
AccessioniPrimary (citable) accession number: Q01082
Secondary accession number(s): B2RP63
, O60837, Q16057, Q53R99, Q59ER3, Q8IX99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 180 of the entry and version 2 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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.