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Q01082

- SPTB2_HUMAN

UniProt

Q01082 - SPTB2_HUMAN

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Protein
Spectrin beta chain, non-erythrocytic 1
Gene
SPTBN1, SPTB2
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. protein binding Source: UniProtKB
  6. structural constituent of cytoskeleton Source: BHF-UCL

GO - Biological processi

  1. Golgi to plasma membrane protein transport Source: BHF-UCL
  2. SMAD protein import into nucleus Source: Ensembl
  3. actin filament capping Source: UniProtKB-KW
  4. axon guidance Source: Reactome
  5. common-partner SMAD protein phosphorylation Source: Ensembl
  6. membrane assembly Source: BHF-UCL
  7. mitotic cytokinesis Source: BHF-UCL
  8. plasma membrane organization Source: BHF-UCL
  9. 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.

GO - Cellular componenti

  1. M band Source: UniProtKB-SubCell
  2. axolemma Source: BHF-UCL
  3. cuticular plate Source: Ensembl
  4. cytoplasm Source: HGNC
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProt
  7. nucleolus Source: HGNC
  8. protein complex Source: Ensembl
  9. spectrin Source: ProtInc
  10. 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 – 11Removed1 Publication
Chaini2 – 23642363Spectrin beta chain, non-erythrocytic 1
PRO_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 – 18051Phosphotyrosine By 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 – 21951Phosphothreonine By 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

ArrayExpressiQ01082.
BgeeiQ01082.
CleanExiHS_SPTBN1.
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. 83 interactions.
DIPiDIP-33182N.
IntActiQ01082. 42 interactions.
MINTiMINT-1136298.
STRINGi9606.ENSP00000349259.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ01082.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1563 – 2093531Interaction with ANK2
Add
BLAST
Regioni2149 – 217729Mediates interaction with CAMSAP1
Add
BLAST

Sequence similaritiesi

Belongs to the spectrin family.
Contains 1 PH domain.
Contains 17 spectrin repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
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

MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD     50
EREAVQKKTF TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL 100
PKPTKGRMRI HCLENVDKAL QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI 150
WTIILRFQIQ DISVETEDNK EKKSAKDALL LWCQMKTAGY PNVNIHNFTT 200
SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL AEQHLGLTKL 250
LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET 300
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV 350
EKPPKFTEKG NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE 400
KAEHERELAL RNELIRQEKL EQLARRFDRK AAMRETWLSE NQRLVSQDNF 450
GFDLPAVEAA TKKHEAIETD IAAYEERVQA VVAVARELEA ENYHDIKRIT 500
ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI MDWMDEMKVL 550
VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG 600
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE 650
EGWIREKEKI LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE 700
GEDMIAEEHF GSEKIRERII YIREQWANLE QLSAIRKKRL EEASLLHQFQ 750
ADADDIDAWM LDILKIVSSS DVGHDEYSTQ SLVKKHKDVA EEIANYRPTL 800
DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL RKQALQDTLA 850
LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 900
QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA 950
LLSALSIQNY HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG 1000
MERDLVAIEA KLSDLQKEAE KLESEHPDQA QAILSRLAEI SDVWEEMKTT 1050
LKNREASLGE ASKLQQFLRD LDDFQSWLSR TQTAIASEDM PNTLTEAEKL 1100
LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL RQRLQALDTG 1150
WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT 1200
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV 1250
DSIDDRHRKN RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD 1300
MSYDEARNLH SKWLKHQAFM AELASNKEWL DKIEKEGMQL ISEKPETEAV 1350
VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN KAELFTQSCA DLDKWLHGLE 1400
SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ SQAQALSQEG 1450
KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW 1500
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN 1550
IVTDSSSLSA EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD 1600
AAEAEAWMSE QELYMMSEEK AKDEQSAVSM LKKHQILEQA VEDYAETVHQ 1650
LSKTSRALVA DSHPESERIS MRQSKVDKLY AGLKDLAEER RGKLDERHRL 1700
FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI 1750
GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 1800
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE 1850
HDIQALGTQV RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC 1900
ESRRVRLVDT GDKFRFFSMV RDLMLWMEDV IRQIEAQEKP RDVSSVELLM 1950
NNHQGIKAEI DARNDSFTTC IELGKSLLAR KHYASEEIKE KLLQLTEKRK 2000
EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL SSREIGQSVD 2050
EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 2100
PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM 2150
VNGATEQRTS SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM 2200
EGFLNRKHEW EAHNKKASSR SWHNVYCVIN NQEMGFYKDA KTAASGIPYH 2250
SEVPVSLKEA VCEVALDYKK KKHVFKLRLN DGNEYLFQAK DDEEMNTWIQ 2300
AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES SPGKREKDKE 2350
KDKEKRFSLF GKKK 2364
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.

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.
VSP_026054Add
BLAST
Alternative sequencei2141 – 222585MAETV…SWHNV → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform 2.
VSP_026055Add
BLAST
Alternative sequencei2141 – 216828MAETV…SSPIP → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform Short.
VSP_000720Add
BLAST
Alternative sequencei2169 – 2364196Missing in isoform Short.
VSP_000721Add
BLAST
Alternative sequencei2226 – 2364139Missing in isoform 2.
VSP_026056Add
BLAST

Sequence conflict

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

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. 83 interactions.
DIPi DIP-33182N.
IntActi Q01082. 42 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.
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

ArrayExpressi Q01082.
Bgeei Q01082.
CleanExi HS_SPTBN1.
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: September 3, 2014
This is version 156 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

Dasty 3

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