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Q01082 (SPTB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. 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, non-erythrocytic 1
Alternative name(s):
Beta-II spectrin
Fodrin beta chain
Spectrin, non-erythroid beta chain 1
Gene names
Name:SPTBN1
Synonyms:SPTB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.9 Ref.24

Subcellular location

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; Peripheral membrane protein; Cytoplasmic side By similarity.

Tissue specificity

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

Sequence similarities

Belongs to the spectrin family.

Contains 2 CH (calponin-homology) domains.

Contains 1 PH domain.

Contains 17 spectrin repeats.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandActin-binding
Calmodulin-binding
   Molecular functionActin capping
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane protein transport

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

SMAD protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

actin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Traceable author statement. Source: Reactome

common-partner SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

membrane assembly

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

mitotic cytokinesis

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

plasma membrane organization

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

protein targeting to plasma membrane

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

   Cellular_componentM band

Inferred from electronic annotation. Source: UniProtKB-SubCell

axolemma

Inferred from sequence or structural similarity. Source: BHF-UCL

cuticular plate

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 9537418. Source: HGNC

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

nucleolus

Inferred from direct assay PubMed 9537418. Source: HGNC

protein complex

Inferred from electronic annotation. Source: Ensembl

spectrin

Traceable author statement Ref.1. Source: ProtInc

spectrin-associated cytoskeleton

Non-traceable author statement PubMed 17620337. Source: BHF-UCL

   Molecular_functionactin binding

Traceable author statement Ref.1. Source: ProtInc

ankyrin binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

phospholipid binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

structural constituent of cytoskeleton

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q01082-1)

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 Short (identifier: Q01082-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2141-2168: MAETVDTSEMVNGATEQRTSSKESSPIP → VSYRSQTYQNYKNFNSRRTASDQPWSGL
     2169-2364: Missing.
Isoform 2 (identifier: Q01082-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 23642363Spectrin beta chain, non-erythrocytic 1
PRO_0000073461

Regions

Domain1 – 275275Actin-binding
Domain54 – 158105CH 1
Domain173 – 275103CH 2
Repeat303 – 411109Spectrin 1
Repeat423 – 525103Spectrin 2
Repeat530 – 636107Spectrin 3
Repeat639 – 742104Spectrin 4
Repeat745 – 847103Spectrin 5
Repeat851 – 952102Spectrin 6
Repeat957 – 1060104Spectrin 7
Repeat1063 – 1166104Spectrin 8
Repeat1169 – 125789Spectrin 9
Repeat1276 – 1376101Spectrin 10
Repeat1381 – 1482102Spectrin 11
Repeat1486 – 1590105Spectrin 12
Repeat1592 – 1696105Spectrin 13
Repeat1698 – 1801104Spectrin 14
Repeat1805 – 1907103Spectrin 15
Repeat1914 – 2014101Spectrin 16
Repeat2018 – 209780Spectrin 17
Domain2197 – 2307111PH
Region1563 – 2093531Interaction with ANK2
Region2149 – 217729Mediates interaction with CAMSAP1

Amino acid modifications

Modified residue21N-acetylthreonine Ref.15 Ref.22 Ref.23
Modified residue901N6-acetyllysine Ref.18
Modified residue8171Phosphoserine Ref.19
Modified residue8251Phosphoserine Ref.19
Modified residue10571Phosphoserine Ref.19
Modified residue14471Phosphoserine Ref.17
Modified residue18051Phosphotyrosine By similarity
Modified residue18151N6-acetyllysine Ref.18
Modified residue19131N6-acetyllysine Ref.18
Modified residue19891N6-acetyllysine Ref.18
Modified residue21021Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.19 Ref.21
Modified residue21281Phosphoserine Ref.21
Modified residue21381Phosphoserine Ref.10 Ref.13 Ref.14 Ref.17 Ref.19 Ref.21
Modified residue21601Phosphoserine Ref.21
Modified residue21611Phosphoserine Ref.21
Modified residue21641Phosphoserine Ref.21
Modified residue21651Phosphoserine Ref.14
Modified residue21691Phosphoserine Ref.14 Ref.17 Ref.19 Ref.21
Modified residue21871Phosphothreonine Ref.14
Modified residue21951Phosphothreonine By similarity
Modified residue23191Phosphoserine Ref.21
Modified residue23201Phosphothreonine Ref.14 Ref.19 Ref.21
Modified residue23281Phosphothreonine Ref.14
Modified residue23401Phosphoserine Ref.21
Modified residue23411Phosphoserine Ref.14 Ref.17 Ref.19
Glycosylation23241O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence1 – 4949MTTTV…IKALA → MELQRTSSISGPLSPAYTGQ VPYNYNQLEGRFKQLQ in isoform 2.
VSP_026054
Alternative sequence2141 – 222585MAETV…SWHNV → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform 2.
VSP_026055
Alternative sequence2141 – 216828MAETV…SSPIP → VSYRSQTYQNYKNFNSRRTA SDQPWSGL in isoform Short.
VSP_000720
Alternative sequence2169 – 2364196Missing in isoform Short.
VSP_000721
Alternative sequence2226 – 2364139Missing in isoform 2.
VSP_026056
Natural variant14111D → H. Ref.1 Ref.2
Corresponds to variant rs1052790 [ dbSNP | Ensembl ].
VAR_032641

Experimental info

Sequence conflict5831R → W in BAD92985. Ref.3

Secondary structure

...................................... 2364
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: 1770C3B0EB07B892

FASTA2,364274,609
        10         20         30         40         50         60 
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF 

        70         80         90        100        110        120 
TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL 

       130        140        150        160        170        180 
QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL 

       190        200        210        220        230        240 
LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL 

       250        260        270        280        290        300 
AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET 

       310        320        330        340        350        360 
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG 

       370        380        390        400        410        420 
NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL 

       430        440        450        460        470        480 
EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA 

       490        500        510        520        530        540 
VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI 

       550        560        570        580        590        600 
MDWMDEMKVL VLSQDYGKHL LGVEDLLQKH TLVEADIGIQ AERVRGVNAS AQKFATDGEG 

       610        620        630        640        650        660 
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI 

       670        680        690        700        710        720 
LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII 

       730        740        750        760        770        780 
YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSS DVGHDEYSTQ 

       790        800        810        820        830        840 
SLVKKHKDVA EEIANYRPTL DTLHEQASAL PQEHAESPDV RGRLSGIEER YKEVAELTRL 

       850        860        870        880        890        900 
RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 

       910        920        930        940        950        960 
QASRVAVVNQ IARQLMHSGH PSEKEIKAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY 

       970        980        990       1000       1010       1020 
HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE 

      1030       1040       1050       1060       1070       1080 
KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR 

      1090       1100       1110       1120       1130       1140 
TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL 

      1150       1160       1170       1180       1190       1200 
RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT 

      1210       1220       1230       1240       1250       1260 
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN 

      1270       1280       1290       1300       1310       1320 
RETASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM 

      1330       1340       1350       1360       1370       1380 
AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN 

      1390       1400       1410       1420       1430       1440 
KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ 

      1450       1460       1470       1480       1490       1500 
SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLNERKHN LLASKEIHQF NRDVEDEILW 

      1510       1520       1530       1540       1550       1560 
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IVTDSSSLSA 

      1570       1580       1590       1600       1610       1620 
EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHRAQQYYFD AAEAEAWMSE QELYMMSEEK 

      1630       1640       1650       1660       1670       1680 
AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY 

      1690       1700       1710       1720       1730       1740 
AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF 

      1750       1760       1770       1780       1790       1800 
REFARDTGNI GQERVDTVNH LADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 

      1810       1820       1830       1840       1850       1860 
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV 

      1870       1880       1890       1900       1910       1920 
RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC ESRRVRLVDT GDKFRFFSMV 

      1930       1940       1950       1960       1970       1980 
RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTTC IELGKSLLAR 

      1990       2000       2010       2020       2030       2040 
KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL 

      2050       2060       2070       2080       2090       2100 
SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 

      2110       2120       2130       2140       2150       2160 
PSPEPSTKVS EEAESQQQWD TSKGEQVSQN GLPAEQGSPR MAETVDTSEM VNGATEQRTS 

      2170       2180       2190       2200       2210       2220 
SKESSPIPSP TSDRKAKTAL PAQSAATLPA RTQETPSAQM EGFLNRKHEW EAHNKKASSR 

      2230       2240       2250       2260       2270       2280 
SWHNVYCVIN NQEMGFYKDA KTAASGIPYH SEVPVSLKEA VCEVALDYKK KKHVFKLRLN 

      2290       2300       2310       2320       2330       2340 
DGNEYLFQAK DDEEMNTWIQ AISSAISSDK HEVSASTQST PASSRAQTLP TSVVTITSES 

      2350       2360 
SPGKREKDKE KDKEKRFSLF GKKK 

« Hide

Isoform Short [UniParc].

Checksum: 34F9C77E47199043
Show »

FASTA2,168253,091
Isoform 2 [UniParc].

Checksum: 2CA864D7AAC0182C
Show »

FASTA2,155251,397

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33198.1. [Q01082-1]
CCDS33199.1. [Q01082-3]
PIRA44159.
A47213.
RefSeqNP_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]
UniGeneHs.503178.
Hs.705692.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AA2X-ray2.00A173-280[»]
1BKRX-ray1.10A172-280[»]
3EDVX-ray1.95A/B1697-2015[»]
ProteinModelPortalQ01082.
SMRQ01082. Positions 48-280, 299-2086, 2200-2305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112589. 83 interactions.
DIPDIP-33182N.
IntActQ01082. 42 interactions.
MINTMINT-1136298.
STRING9606.ENSP00000349259.

PTM databases

PhosphoSiteQ01082.

Polymorphism databases

DMDM116242799.

Proteomic databases

MaxQBQ01082.
PaxDbQ01082.
PRIDEQ01082.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333896; ENSP00000334156; ENSG00000115306. [Q01082-3]
ENST00000356805; ENSP00000349259; ENSG00000115306. [Q01082-1]
GeneID6711.
KEGGhsa:6711.
UCSCuc002rxu.3. human. [Q01082-1]
uc002rxx.3. human. [Q01082-3]

Organism-specific databases

CTD6711.
GeneCardsGC02P054665.
H-InvDBHIX0002055.
HGNCHGNC:11275. SPTBN1.
HPAHPA012685.
HPA013149.
MIM182790. gene.
neXtProtNX_Q01082.
PharmGKBPA36104.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOVERGENHBG057912.
InParanoidQ01082.
KOK06115.
OMALWQFYWD.
OrthoDBEOG73RB9J.
PhylomeDBQ01082.
TreeFamTF313446.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_188576. Developmental Biology.
SignaLinkQ01082.

Gene expression databases

ArrayExpressQ01082.
BgeeQ01082.
CleanExHS_SPTBN1.
GenevestigatorQ01082.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001605. PH_dom-spectrin-type.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF00169. PH. 1 hit.
PF00435. Spectrin. 17 hits.
[Graphical view]
PIRSFPIRSF002297. Spectrin_beta_subunit. 1 hit.
PRINTSPR00683. SPECTRINPH.
SMARTSM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPTBN1. human.
EvolutionaryTraceQ01082.
GeneWikiSPTBN1.
GenomeRNAi6711.
NextBio26172.
PROQ01082.
SOURCESearch...

Entry information

Entry nameSPTB2_HUMAN
AccessionPrimary (citable) accession number: Q01082
Secondary accession number(s): B2RP63 expand/collapse secondary AC list , O60837, Q16057, Q53R99, Q59ER3, Q8IX99
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 155 of the entry and version 2 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 2

Human chromosome 2: entries, gene names and cross-references to MIM