CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002588
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spectrin alpha chain, erythrocytic 1 
Protein Synonyms/Alias
 Erythroid alpha-spectrin 
Gene Name
 Spta1 
Gene Synonyms/Alias
 Spna1; Spta 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
615YKDVQNLKSRVQKQQubiquitination[1]
698ENNAEDLKRWLEEVEubiquitination[1]
1645TSAGNLLKKHQLLEAubiquitination[1]
1905KIQVLNEKTASLAKAacetylation[2]
2270GVSEETLKEFSTTYKubiquitination[1]
2277KEFSTTYKHFDENLTubiquitination[1]
2317EPEPKFEKFLNAVDPubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 
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. 
Sequence Annotation
 REPEAT 18 50 Spectrin 1.
 REPEAT 52 154 Spectrin 2.
 REPEAT 156 260 Spectrin 3.
 REPEAT 262 366 Spectrin 4.
 REPEAT 368 472 Spectrin 5.
 REPEAT 474 578 Spectrin 6.
 REPEAT 580 683 Spectrin 7.
 REPEAT 685 789 Spectrin 8.
 REPEAT 791 895 Spectrin 9.
 REPEAT 897 966 Spectrin 10.
 DOMAIN 975 1034 SH3.
 REPEAT 1080 1179 Spectrin 11.
 REPEAT 1181 1285 Spectrin 12.
 REPEAT 1287 1391 Spectrin 13.
 REPEAT 1393 1496 Spectrin 14.
 REPEAT 1498 1603 Spectrin 15.
 REPEAT 1605 1709 Spectrin 16.
 REPEAT 1711 1815 Spectrin 17.
 REPEAT 1817 1922 Spectrin 18.
 REPEAT 1924 2029 Spectrin 19.
 REPEAT 2039 2143 Spectrin 20.
 REPEAT 2153 2254 Spectrin 21.
 DOMAIN 2267 2302 EF-hand 1.
 DOMAIN 2310 2345 EF-hand 2.
 DOMAIN 2347 2382 EF-hand 3.  
Keyword
 Actin capping; Actin-binding; Calcium; Cell shape; Complete proteome; Cytoplasm; Cytoskeleton; Metal-binding; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2415 AA 
Protein Sequence
METPKETAVE SSGPKVLETA EEIQHRRAEV LNQYQRFKDR VAERGQKLEE SYHYQVFRRD 60
ADDLEKWIME KLEIAKDKTY EPTNIQGKYQ KHESFVSEVQ AKSRVLPELE EIREARFAED 120
HFAHEATKTH LKQLRLLWDL LLELTQEKSD VLLRALKFYQ YSQECEDILE WVKEKEAIVT 180
LVELGDDWER TEVLHKKFEE FQEELTARKG KVDRVNQYAN ECAQEKHPKL PEIKAKQDEV 240
NAAWDRLWSL ALKRRESLSN AADLQRFKRD VNEAIQWMEE KEPQLTSEDY GKDLVSSEAL 300
FHNHKRLERN LAVMDDKVKE LCAKADKLMI SHSADAPQIQ QMKLDLVSNW ERIRALATNR 360
YAKLKASYGY HRFLSDYDEL SGWMKEKTAL INADELPTDV ASGEALLARH QQHKHEIDSY 420
DDRFQSADAT GQELLDGNHE ASEEIREKMT ILANDWAALL ELWDKCQHQY RQCLDFHLFY 480
RDSEQVDSWM SRQEAFLENE DLGNSVGSVE ALLQKHDDFE EAFTAQEEKI ITLDETATKL 540
IDNDHYDSEN IAAIRDGLLA RRDALRERAA TRRKLLVDSQ LLQQLYQDSD DLKTWINKKK 600
KLADDDDYKD VQNLKSRVQK QQDFEEELAV NEIMLNNLEK TGQEMIEDGH YASEAVAARL 660
SEVANLWKEL LEATAQKGTQ LYEANQLLQF ENNAEDLKRW LEEVEWQVTS EDYGKGLADV 720
QNLLRKHGLL ESDVTARQNQ VDTLTDMAAH FEEIGHPDSG DIRARQESLL SRFEALKEPL 780
AIRKKKLIDL LKLQQICRDS EDEEAWIQET EPSAASTHLG KDLVAAKNLL NRHEVILADI 840
ASHEPRIQVI TERGNKMVEE GHFAAEDIAS RVESLNKNME SLHARAIRRE NDLKANVQLQ 900
QYLADLHEAE AWIKEKEPIV DNKNYGADEE AAGALLKKHE AFLVDLNAFE NSIKALRDQA 960
EVCQQQQAAP VDEAGREARV IALYDFEARS RREVSMKKND VLTLLSSINK DWWKVEADDH 1020
QGFVPAVYVR KLAPDELPGF PQHRQEEPVN IPQLQQQVET LYHSLLDRAE ERRRRLLQRY 1080
NEFLLAYEAG DMLEWIQEKK TENTGVELDD VWELQKKFDE FQRDLKSNEP RLKDINKVAD 1140
ELLFEELLTP EGAHIRQELN TRWNSLKRLA DEQYQLLSSA HAVEMFHREA DDVKEQIDKK 1200
CRALNAADPG SDLLSVQALQ RQHEVFERDI IPLGEKVTTL GETAERLCES HPDATEDLQK 1260
QRTELNEAWD TLQGLTSDRK ESLNEAHKFF LFLSKASDLE NWIKTIGGVI SSPELAEDLT 1320
GTEILLERHQ EHHDDIKRED PTFQALEDFG TELIDSGHRN RREIDNTLQN INSKRDNLEK 1380
SWENRKKMLD QCLELQLFRG KCDQVESWMV ARENSLRSDD RDHLNSLQAL MKKRDDLDKA 1440
ITAQEGKISD LENVATRLID NDHYAKEEIA ARLQRVLDRW KALKEQLLTE LGKLGDYADL 1500
KQFYRDLEDL EEWINEMLPI ACDESYKDPT NIQRKYLKHQ AFENEVNGRA EQVDGVINLG 1560
NSLIERRVCD GDEENMQEQL DKLKENWDYL LERTTDKGQK LNEASRQQRF NTSIRDFEFW 1620
LSEAEGLLAM KDQARDLTSA GNLLKKHQLL EAEMLAREDP LKDLNDLAQE LISSGTFNID 1680
QIEEKMNGVN ERFENVQSLA AAHHEKLKET YALFQFFQDL DDEEAWIEEK LLRVSSQDYG 1740
RDLQSVQNLL KKHKRLEGEL VAHEPAVQNV LDTAESLRDK AAVGKEEIQE RLAQFVQHWE 1800
KLKELAKTRG VNLEESLEYL QFMENAEEEE AWLGEKCALV SRGDSGDTLA ATQSLLKKHE 1860
ALENDFAVHK NRVQDVCAQG EDILNKEETQ NKDKISTKIQ VLNEKTASLA KALAAWKSQL 1920
DDVHAFQQFN WKADVVESWI GEKEASLKTK SNGADLTAFL TLLAKHDTLD ASLQSFQQER 1980
LSEIAELKDQ LVAGEHSQAK AIEEQHAALL RHWEQLLEAS RVHRQKLLEK QLPLQKAEEL 2040
FMEFAHKASA FNNWCENAEE DLSEPVHCVS LNEIRQLQKE HEAFLASLAG AQEDFNYLLE 2100
LDKQIKALNV PSSPYTWLTV DVLGRIWNHL PDIIKEREQE LQKEEARQIK NFEMCQEFEQ 2160
NASAFLQWIQ ETRAYFLDGS LLKETGTLES QLEANKRKQK EIQAMKRHLT KIEDLGDSME 2220
EALILDIKYS TIGLAQQWDQ LHQLGMRMQH NLEQQIQAKD TIGVSEETLK EFSTTYKHFD 2280
ENLTGRLTHK EFRSCLRGLN YYLPMVEEGE PEPKFEKFLN AVDPGRKGYV SLEDYTSFLI 2340
DKESENIKTS DDIESAFQAL AEGKAYITKE DMKQALTPEQ VSFCTIHMQQ YMDPRGRSQP 2400
AGYDYVGFTN SFFGN 2415 
Gene Ontology
 GO:0032437; C:cuticular plate; IDA:MGI.
 GO:0016020; C:membrane; IDA:MGI.
 GO:0008091; C:spectrin; IMP:MGI.
 GO:0014731; C:spectrin-associated cytoskeleton; IMP:MGI.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0030097; P:hemopoiesis; IMP:MGI.
 GO:0002260; P:lymphocyte homeostasis; IMP:MGI.
 GO:0007009; P:plasma membrane organization; IMP:MGI.
 GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:MGI.
 GO:0032092; P:positive regulation of protein binding; IGI:MGI.
 GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
 GO:0008360; P:regulation of cell shape; IMP:MGI. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR014837; EF-hand_Ca_insen.
 IPR002048; EF_hand_dom.
 IPR001452; SH3_domain.
 IPR018159; Spectrin/alpha-actinin.
 IPR013315; Spectrin_alpha_SH3.
 IPR002017; Spectrin_repeat. 
Pfam
 PF08726; efhand_Ca_insen
 PF00018; SH3_1
 PF00435; Spectrin 
SMART
 SM00326; SH3
 SM00150; SPEC 
PROSITE
 PS50222; EF_HAND_2
 PS50002; SH3 
PRINTS
 PR01887; SPECTRNALPHA.