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Q01082

- SPTB2_HUMAN

UniProt

Q01082 - SPTB2_HUMAN

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Protein

Spectrin beta chain, non-erythrocytic 1

Gene

SPTBN1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. actin binding Source: ProtInc
  2. ankyrin binding Source: BHF-UCL
  3. phospholipid binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
  5. structural constituent of cytoskeleton Source: BHF-UCL

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. axon guidance Source: Reactome
  3. Golgi to plasma membrane protein transport Source: BHF-UCL
  4. membrane assembly Source: BHF-UCL
  5. mitotic cytokinesis Source: BHF-UCL
  6. plasma membrane organization Source: BHF-UCL
  7. protein targeting to plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_18334. NCAM signaling for neurite out-growth.
REACT_22266. Interaction between L1 and Ankyrins.
REACT_23832. Nephrin interactions.
SignaLinkiQ01082.

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
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:11275. SPTBN1.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. CytoplasmmyofibrilsarcomereM line By similarity
Note: Colocalizes with ANK2 in a distinct intracellular compartment of neonatal cardiomyocytes.By similarity
Isoform 2 : Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

GO - Cellular componenti

  1. axolemma Source: BHF-UCL
  2. cytoplasm Source: HGNC
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. nucleolus Source: HGNC
  6. protein complex Source: Ensembl
  7. spectrin Source: ProtInc
  8. spectrin-associated cytoskeleton Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36104.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 23642363Spectrin beta chain, non-erythrocytic 1PRO_0000073461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine3 Publications
Modified residuei90 – 901N6-acetyllysine1 Publication
Modified residuei817 – 8171Phosphoserine1 Publication
Modified residuei825 – 8251Phosphoserine1 Publication
Modified residuei1057 – 10571Phosphoserine1 Publication
Modified residuei1447 – 14471Phosphoserine1 Publication
Modified residuei1805 – 18051PhosphotyrosineBy similarity
Modified residuei1815 – 18151N6-acetyllysine1 Publication
Modified residuei1913 – 19131N6-acetyllysine1 Publication
Modified residuei1989 – 19891N6-acetyllysine1 Publication
Modified residuei2102 – 21021Phosphoserine7 Publications
Modified residuei2128 – 21281Phosphoserine1 Publication
Modified residuei2138 – 21381Phosphoserine6 Publications
Modified residuei2160 – 21601Phosphoserine1 Publication
Modified residuei2161 – 21611Phosphoserine1 Publication
Modified residuei2164 – 21641Phosphoserine1 Publication
Modified residuei2165 – 21651Phosphoserine1 Publication
Modified residuei2169 – 21691Phosphoserine4 Publications
Modified residuei2187 – 21871Phosphothreonine1 Publication
Modified residuei2195 – 21951PhosphothreonineBy similarity
Modified residuei2319 – 23191Phosphoserine1 Publication
Modified residuei2320 – 23201Phosphothreonine3 Publications
Glycosylationi2324 – 23241O-linked (GlcNAc)By similarity
Modified residuei2328 – 23281Phosphothreonine1 Publication
Modified residuei2340 – 23401Phosphoserine1 Publication
Modified residuei2341 – 23411Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ01082.
PaxDbiQ01082.
PRIDEiQ01082.

PTM databases

PhosphoSiteiQ01082.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ01082.
CleanExiHS_SPTBN1.
ExpressionAtlasiQ01082. baseline and differential.
GenevestigatoriQ01082.

Organism-specific databases

HPAiHPA012685.
HPA013149.

Interactioni

Subunit structurei

Like erythrocyte spectrin, the spectrin-like proteins are capable to form dimers which can further associate to tetramers. Interacts with CAMSAP1. Interacts with ANK2. Isoform Short cannot bind to the axonal protein fodaxin.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112589. 85 interactions.
DIPiDIP-33182N.
IntActiQ01082. 46 interactions.
MINTiMINT-1136298.
STRINGi9606.ENSP00000349259.

Structurei

Secondary structure

1
2364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi174 – 18613
Turni187 – 1893
Beta strandi196 – 1994
Helixi200 – 2023
Helixi206 – 21510
Helixi217 – 2193
Helixi222 – 2243
Helixi230 – 24516
Helixi253 – 2564
Beta strandi257 – 2604
Helixi263 – 27715
Helixi1697 – 172125
Helixi1730 – 176738
Helixi1773 – 182654
Helixi1836 – 185217
Helixi1854 – 187320
Helixi1877 – 193559
Helixi1943 – 196220
Helixi1964 – 197916
Helixi1985 – 201430

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA2X-ray2.00A173-280[»]
1BKRX-ray1.10A172-280[»]
3EDVX-ray1.95A/B1697-2015[»]
ProteinModelPortaliQ01082.
SMRiQ01082. Positions 48-280, 299-2086, 2200-2305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01082.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 275275Actin-bindingAdd
BLAST
Domaini54 – 158105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini173 – 275103CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati303 – 411109Spectrin 1Add
BLAST
Repeati423 – 525103Spectrin 2Add
BLAST
Repeati530 – 636107Spectrin 3Add
BLAST
Repeati639 – 742104Spectrin 4Add
BLAST
Repeati745 – 847103Spectrin 5Add
BLAST
Repeati851 – 952102Spectrin 6Add
BLAST
Repeati957 – 1060104Spectrin 7Add
BLAST
Repeati1063 – 1166104Spectrin 8Add
BLAST
Repeati1169 – 125789Spectrin 9Add
BLAST
Repeati1276 – 1376101Spectrin 10Add
BLAST
Repeati1381 – 1482102Spectrin 11Add
BLAST
Repeati1486 – 1590105Spectrin 12Add
BLAST
Repeati1592 – 1696105Spectrin 13Add
BLAST
Repeati1698 – 1801104Spectrin 14Add
BLAST
Repeati1805 – 1907103Spectrin 15Add
BLAST
Repeati1914 – 2014101Spectrin 16Add
BLAST
Repeati2018 – 209780Spectrin 17Add
BLAST
Domaini2197 – 2307111PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1563 – 2093531Interaction with ANK2Add
BLAST
Regioni2149 – 217729Mediates interaction with CAMSAP1Add
BLAST

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

eggNOGiCOG5069.
GeneTreeiENSGT00760000118813.
HOVERGENiHBG057912.
InParanoidiQ01082.
KOiK06115.
OMAiLWQFYWD.
OrthoDBiEOG73RB9J.
PhylomeDBiQ01082.
TreeFamiTF313446.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001605. PH_dom-spectrin-type.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00169. PH. 1 hit.
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.
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. Align

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.

Note: Contains a phosphoserine at position 14.

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

Sequence cautioni

The sequence BAD92985.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti583 – 5831R → W in BAD92985. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1411 – 14111D → H.2 Publications
Corresponds to variant rs1052790 [ dbSNP | Ensembl ].
VAR_032641

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949MTTTV…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2. 2 PublicationsVSP_026054Add
BLAST
Alternative sequencei2141 – 222585MAETV…SWHNV → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform 2. 2 PublicationsVSP_026055Add
BLAST
Alternative sequencei2141 – 216828MAETV…SSPIP → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform Short. 1 PublicationVSP_000720Add
BLAST
Alternative sequencei2169 – 2364196Missing in isoform Short. 1 PublicationVSP_000721Add
BLAST
Alternative sequencei2226 – 2364139Missing in isoform 2. 2 PublicationsVSP_026056Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005264517.1. [Q01082-1]
XP_006712150.1. XM_006712087.1. [Q01082-1]
UniGeneiHs.503178.
Hs.705692.

Genome annotation databases

EnsembliENST00000333896; ENSP00000334156; ENSG00000115306. [Q01082-3]
ENST00000356805; ENSP00000349259; ENSG00000115306. [Q01082-1]
GeneIDi6711.
KEGGihsa:6711.
UCSCiuc002rxu.3. human. [Q01082-1]
uc002rxx.3. human. [Q01082-3]

Polymorphism databases

DMDMi116242799.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS33198.1. [Q01082-1 ]
CCDS33199.1. [Q01082-3 ]
PIRi A44159.
A47213.
RefSeqi NP_003119.2. NM_003128.2. [Q01082-1 ]
NP_842565.2. NM_178313.2. [Q01082-3 ]
XP_005264574.1. XM_005264517.1. [Q01082-1 ]
XP_006712150.1. XM_006712087.1. [Q01082-1 ]
UniGenei Hs.503178.
Hs.705692.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AA2 X-ray 2.00 A 173-280 [» ]
1BKR X-ray 1.10 A 172-280 [» ]
3EDV X-ray 1.95 A/B 1697-2015 [» ]
ProteinModelPortali Q01082.
SMRi Q01082. Positions 48-280, 299-2086, 2200-2305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112589. 85 interactions.
DIPi DIP-33182N.
IntActi Q01082. 46 interactions.
MINTi MINT-1136298.
STRINGi 9606.ENSP00000349259.

PTM databases

PhosphoSitei Q01082.

Polymorphism databases

DMDMi 116242799.

Proteomic databases

MaxQBi Q01082.
PaxDbi Q01082.
PRIDEi Q01082.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000333896 ; ENSP00000334156 ; ENSG00000115306 . [Q01082-3 ]
ENST00000356805 ; ENSP00000349259 ; ENSG00000115306 . [Q01082-1 ]
GeneIDi 6711.
KEGGi hsa:6711.
UCSCi uc002rxu.3. human. [Q01082-1 ]
uc002rxx.3. human. [Q01082-3 ]

Organism-specific databases

CTDi 6711.
GeneCardsi GC02P054665.
H-InvDB HIX0002055.
HGNCi HGNC:11275. SPTBN1.
HPAi HPA012685.
HPA013149.
MIMi 182790. gene.
neXtProti NX_Q01082.
PharmGKBi PA36104.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000118813.
HOVERGENi HBG057912.
InParanoidi Q01082.
KOi K06115.
OMAi LWQFYWD.
OrthoDBi EOG73RB9J.
PhylomeDBi Q01082.
TreeFami TF313446.

Enzyme and pathway databases

Reactomei REACT_18334. NCAM signaling for neurite out-growth.
REACT_22266. Interaction between L1 and Ankyrins.
REACT_23832. Nephrin interactions.
SignaLinki Q01082.

Miscellaneous databases

ChiTaRSi SPTBN1. human.
EvolutionaryTracei Q01082.
GeneWikii SPTBN1.
GenomeRNAii 6711.
NextBioi 26172.
PROi Q01082.
SOURCEi Search...

Gene expression databases

Bgeei Q01082.
CleanExi HS_SPTBN1.
ExpressionAtlasi Q01082. baseline and differential.
Genevestigatori Q01082.

Family and domain databases

Gene3Di 1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001605. PH_dom-spectrin-type.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view ]
Pfami PF00307. CH. 2 hits.
PF00169. PH. 1 hit.
PF00435. Spectrin. 17 hits.
[Graphical view ]
PIRSFi PIRSF002297. Spectrin_beta_subunit. 1 hit.
PRINTSi PR00683. SPECTRINPH.
SMARTi SM00033. CH. 2 hits.
SM00233. PH. 1 hit.
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.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of human brain cDNA encoding the general isoform of beta-spectrin."
    Hu R.J., Watanabe M., Bennett V.
    J. Biol. Chem. 267:18715-18722(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT HIS-1411.
    Tissue: Brain.
  2. "A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin."
    Chen Y., Yu P., Lu D., Tagle D.A., Cai T.
    J. Mol. Neurosci. 17:59-70(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, VARIANT HIS-1411.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
    Tissue: Brain.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  7. "Cloning of a portion of the chromosomal gene and cDNA for human beta-fodrin, the nonerythroid form of beta-spectrin."
    Chang J.G., Scarpa A., Eddy R.L., Byers M.G., Harris A.S., Morrow J.S., Watkins P., Shows T.B., Forget B.G.
    Genomics 17:287-293(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 293-1544.
  8. "Identification of a novel C-terminal variant of betaII spectrin: two isoforms of betaII spectrin have distinct intracellular locations and activities."
    Hayes N.V.L., Scott C., Heerkens E., Ohanian V., Maggs A.M., Pinder J.C., Kordeli E., Baines A.J.
    J. Cell Sci. 113:2023-2034(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2087-2168 (ISOFORM SHORT).
    Tissue: Skeletal muscle.
  9. "Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes."
    Mohler P.J., Yoon W., Bennett V.
    J. Biol. Chem. 279:40185-40193(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANK2.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102 AND SER-2138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2138; SER-2165; SER-2169; THR-2187; THR-2320; THR-2328 AND SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1447; SER-2138; SER-2169 AND SER-2341, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-1815; LYS-1913 AND LYS-1989, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-825; SER-1057; SER-2102; SER-2138; SER-2169; THR-2320 AND SER-2341, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102; SER-2128; SER-2138; SER-2160; SER-2161; SER-2164; SER-2169; SER-2319; THR-2320 AND SER-2340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "A conserved sequence in CAMSAP1 (calmodulin regulated spectrin-associated protein 1) links its interaction with spectrin and calmodulin to neurite outgrowth."
    King M.D., Phillips G.W., Bignone P.A., Hayes N.V., Pinder J.C., Baines A.J.
    J. Neurochem. 128:391-402(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAMSAP1.
  25. "Crystal structure of a calponin homology domain."
    Carugo K.D., Banuelos S., Saraste M.
    Nat. Struct. Biol. 4:175-179(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 173-280.
  26. "Structural comparisons of calponin homology domains: implications for actin binding."
    Banuelos S., Saraste M., Carugo K.D.
    Structure 6:1419-1431(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 173-281.

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: October 29, 2014
This is version 158 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

External Data

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