CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010803
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spectrin beta chain 
Protein Synonyms/Alias
  
Gene Name
 beta-Spec 
Gene Synonyms/Alias
 Spec-b; CG5870 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
2174ASNRSWDKVYMAAKAacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702] 
Functional Description
 Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Interacts with calmodulin in a calcium-dependent manner. 
Sequence Annotation
 DOMAIN 1 271 Actin-binding.
 DOMAIN 50 154 CH 1.
 DOMAIN 169 271 CH 2.
 REPEAT 298 408 Spectrin 1.
 REPEAT 418 522 Spectrin 2.
 REPEAT 524 633 Spectrin 3.
 REPEAT 635 739 Spectrin 4.
 REPEAT 741 844 Spectrin 5.
 REPEAT 846 950 Spectrin 6.
 REPEAT 952 1057 Spectrin 7.
 REPEAT 1059 1167 Spectrin 8.
 REPEAT 1169 1273 Spectrin 9.
 REPEAT 1275 1378 Spectrin 10.
 REPEAT 1380 1485 Spectrin 11.
 REPEAT 1487 1591 Spectrin 12.
 REPEAT 1593 1697 Spectrin 13.
 REPEAT 1699 1804 Spectrin 14.
 REPEAT 1806 1910 Spectrin 15.
 REPEAT 1912 2016 Spectrin 16.
 REPEAT 2018 2078 Spectrin 17.
 DOMAIN 2147 2259 PH.
 MOD_RES 2195 2195 Phosphoserine.  
Keyword
 3D-structure; Actin capping; Actin-binding; Calmodulin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2291 AA 
Protein Sequence
MTTDISIVRW DPSQGPGNEY IDEYEYDGGN SSSRLFERSR IKALAEERES VQKKTFTKWV 60
NSHLCRVNCR IADLYVDMRD GKHLIKLLEV LSGERLPKPT KGKMRIHCLE NVDKALQFLR 120
EQRVHLENIG SHDIVDGNAS LNLGLIWTII LRFQIQDITI EEVDNKETKS AKDALLLWCQ 180
MKTAGYHNVN VRNFTTSWRD GLAFNAIIHK HRPDLVQFEK LSKTNAIHNL NNAFDVAEDK 240
LGLAKLLDAE DVFVEHPDEK SIITYVVTYY HYFSKLKQET VQGKRIGKVV GIAMENDKMV 300
HDYENFTSDL LKWIETTIQS LGEREFENSL AGVQGQLAQF SNYRTIEKPP KFVEKGNLEV 360
LLFTLQSKMR ANNQKPYTPK EGKMISDINK AWERLEKAEH ERELALREEL IRQEKLEQLA 420
ARFDRKASMR ETWLSENQRL VSQDNFGFDL AAVEAAAKKH EAIETDIFAY EERVQAVVAV 480
CDELESERYH DVKRILLRKD NVMRLWTYLL ELLRARRMRL EISLQLQQNF QEMLYILDNM 540
EEIKQLLMTD DYGKHLMGVE DLLQKHSLVE ADINILGERV KVVVQNSQKF LSDDPESYKP 600
CDPEIIVSRV QQLEDAYAEL VRLAVERRSR LEESRKLWQF YWDTADEENW IKEKEQIVST 660
DEVGHDLTTV NLMLSKHKAL ESEITSHDPQ LQNVAKVGSE LITEGHFGAD RIKDRLKEIL 720
NKWDHLLDLT KYRRQRLENA VEYFQLFADA DDVDNWMLDT LRIVSSEDVG RDEANVQSLL 780
KKHKDVADEL KNYAEVIDAL HKQAESLKLN EAEKANVDKR LEAIDNRYKE LTELAKLRKQ 840
RLLDALSLYK LMSEADGVEQ WIKEKTKMLD TMTPGKDIED VEIMKHRFEG FDKEMNANAS 900
RVAVVNQLAR QLLHVEHPNS DEILERQNHL NQEWSTLREK AEAKMDDLKS AHGVQTFYIE 960
CRETISWIED KKRILTETDS LEMDLTGVMT LQRRLSGMDR DLAAIQAKLS SLEREANSIE 1020
DEHPEEAKII RERIAQIELI WEQLTQMLKE RDSKLEEAGD LHRFLRDLDH FQTWLTKTQT 1080
DVASEDTPTS LPEAEKLLNQ HQSIREEIDN YTEDYKNMME YGERLTSEGS TSDDPQYMFL 1140
RERLNALKDG WEELHQMWEN RQVLLSQSLD QQLFNRDARQ TEVLLSQQEH FLSKDDTPVN 1200
LEQAENQLKR HEAFLTTMEA NDDKINTLLQ VADTLVEKDH FDADKIGKRA ENITGRRDDN 1260
RQRALDQHEK LKNQVKLHEF LQDLEELAEW VQEKYATSQD ESYRSAKTIH SKWTRHQAFE 1320
AEIAANKERL FEAEKSAQEL SKEKPEFKDV IEPKLKELAK QFDDLEVHTK EKGAMLFDAN 1380
REVLVQQTCD DIDSYITDLE KQIVSGDTAN DLTSVNILMQ KQQVIQTQMA VKARQVEEID 1440
KQTEYLQKTV PEEKIEPIVV KKTAVLERFE KIKAPLLERQ KALEKKKEAF QFCRDVEDEK 1500
LWIDEKLPVA NSPDYGNSLF NVHVLKKKNQ SLATEIDNHE PRINAICNNG RKLIDEGHED 1560
AKKFEALISD LTQKWQELKD AIENRRKHLL ESEKVQQYFF DAQEAESWMS EQELYMMVED 1620
RGKDEISAQN LMKKHENLEQ SVEDYANTIR QLGEVARQFS GDDISSGDAV AVKQSQLDKL 1680
YAGLKDLAGE RRARLNEALQ LFMLSREVDD LEQWITDREV VAGSQELGQD FDHVTLLSER 1740
FNEFARDTEA VGGERVAKVN GIADNLIQAG HSDSATIAEW KDNLNESWQD LLELIETRTQ 1800
MLAASRELHK FFHDCKDVLG RILEKQHGVS DELGRDAGSV STLQRKHYNF LQDLITLYSQ 1860
VQQIQEESAK LQDAYAGDKA KEITNREQEV LHAWDNLQAM CDARKQKLAD TGDLFRFFNM 1920
VRILMIWMED LVRQMNTSEK PRDVSGVELL MNNHQSLKAE IDTREDNFGA CISLGKELLT 1980
RNHYASADIK DRLMTLSNSR NALLRRWEER WENLQLILEV YQFARDAAVA EAWLIAQEPY 2040
LLSSELGHTI DEVENLIKKH EAFEKSAAAQ EERFSALERL TTFELKEMKR RQELAEEAER 2100
QRIKEEQEAK AASEAAEQAK REAERRDDVD VGASHDDSER GGTPGAGEGH EGYVTRKHEW 2160
DSTTKKASNR SWDKVYMAAK AGRISFYKDQ KGYKSNPELT FRGEPSYDLQ NAAIEIASDY 2220
TKKKHVLRVK LANGALFLLQ AHDDTEMSQW VTSLKAQSDS TAVAASRSQT LPATSQKDEP 2280
KRRSFFTLKK K 2291 
Gene Ontology
 GO:0016327; C:apicolateral plasma membrane; TAS:FlyBase.
 GO:0030424; C:axon; IDA:FlyBase.
 GO:0045169; C:fusome; IDA:FlyBase.
 GO:0016328; C:lateral plasma membrane; IDA:FlyBase.
 GO:0005811; C:lipid particle; IDA:FlyBase.
 GO:0031594; C:neuromuscular junction; IDA:FlyBase.
 GO:0008091; C:spectrin; ISS:FlyBase.
 GO:0045170; C:spectrosome; IDA:FlyBase.
 GO:0003779; F:actin binding; ISS:FlyBase.
 GO:0030506; F:ankyrin binding; IDA:FlyBase.
 GO:0008017; F:microtubule binding; IDA:FlyBase.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:FlyBase.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
 GO:0045478; P:fusome organization; TAS:FlyBase.
 GO:0042062; P:long-term strengthening of neuromuscular junction; IMP:FlyBase.
 GO:0048790; P:maintenance of presynaptic active zone structure; IDA:FlyBase.
 GO:0007026; P:negative regulation of microtubule depolymerization; IMP:FlyBase.
 GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
 GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
 GO:0007009; P:plasma membrane organization; TAS:FlyBase.
 GO:0030721; P:spectrosome organization; TAS:FlyBase. 
Interpro
 IPR001589; 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. 
Pfam
 PF00307; CH
 PF00169; PH
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00233; PH
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS50003; PH_DOMAIN 
PRINTS
 PR00683; SPECTRINPH.