CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001977
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
 SPTA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
283AIQWIKEKEPVLTSEacetylation[1]
1803QFVEHWEKLKELAKAubiquitination[2]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
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 19 51 Spectrin 1.
 REPEAT 53 156 Spectrin 2.
 REPEAT 158 262 Spectrin 3.
 REPEAT 264 368 Spectrin 4.
 REPEAT 370 474 Spectrin 5.
 REPEAT 476 580 Spectrin 6.
 REPEAT 582 685 Spectrin 7.
 REPEAT 687 791 Spectrin 8.
 REPEAT 793 897 Spectrin 9.
 REPEAT 899 968 Spectrin 10.
 DOMAIN 977 1036 SH3.
 REPEAT 1082 1181 Spectrin 11.
 REPEAT 1183 1287 Spectrin 12.
 REPEAT 1289 1393 Spectrin 13.
 REPEAT 1395 1498 Spectrin 14.
 REPEAT 1500 1605 Spectrin 15.
 REPEAT 1607 1711 Spectrin 16.
 REPEAT 1713 1817 Spectrin 17.
 REPEAT 1819 1926 Spectrin 18.
 REPEAT 1928 2033 Spectrin 19.
 REPEAT 2043 2147 Spectrin 20.
 REPEAT 2157 2258 Spectrin 21.
 DOMAIN 2271 2306 EF-hand 1.
 DOMAIN 2314 2349 EF-hand 2.
 DOMAIN 2352 2386 EF-hand 3.  
Keyword
 3D-structure; Actin capping; Actin-binding; Alternative splicing; Calcium; Cell shape; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Elliptocytosis; Hereditary hemolytic anemia; Metal-binding; Polymorphism; Pyropoikilocytosis; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2419 AA 
Protein Sequence
MEQFPKETVV ESSGPKVLET AEEIQERRQE VLTRYQSFKE RVAERGQKLE DSYHLQVFKR 60
DADDLGKWIM EKVNILTDKS YEDPTNIQGK YQKHQSLEAE VQTKSRLMSE LEKTREERFT 120
MGHSAHEETK AHIEELRHLW DLLLELTLEK GDQLLRALKF QQYVQECADI LEWIGDKEAI 180
ATSVELGEDW ERTEVLHKKF EDFQVELVAK EGRVVEVNQY ANECAEENHP DLPLIQSKQN 240
EVNAAWERLR GLALQRQKAL SNAANLQRFK RDVTEAIQWI KEKEPVLTSE DYGKDLVASE 300
GLFHSHKGLE RNLAVMSDKV KELCAKAEKL TLSHPSDAPQ IQEMKEDLVS SWEHIRALAT 360
SRYEKLQATY WYHRFSSDFD ELSGWMNEKT AAINADELPT DVAGGEVLLD RHQQHKHEID 420
SYDDRFQSAD ETGQDLVNAN HEASDEVREK MEILDNNWTA LLELWDERHR QYEQCLDFHL 480
FYRDSEQVDS WMSRQEAFLE NEDLGNSLGS AEALLQKHED FEEAFTAQEE KIITVDKTAT 540
KLIGDDHYDS ENIKAIRDGL LARRDALREK AATRRRLLKE SLLLQKLYED SDDLKNWINK 600
KKKLADDEDY KDIQNLKSRV QKQQVFEKEL AVNKTQLENI QKTGQEMIEG GHYASDNVTT 660
RLSEVASLWE ELLEATKQKG TQLHEANQQL QFENNAEDLQ RWLEDVEWQV TSEDYGKGLA 720
EVQNRLRKHG LLESAVAARQ DQVDILTDLA AYFEEIGHPD SKDIRARQES LVCRFEALKE 780
PLATRKKKLL DLLHLQLICR DTEDEEAWIQ ETEPSATSTY LGKDLIASKK LLNRHRVILE 840
NIASHEPRIQ EITERGNKMV EEGHFAAEDV ASRVKSLNQN MESLRARAAR RQNDLEANVQ 900
FQQYLADLHE AETWIREKEP IVDNTNYGAD EEAAGALLKK HEAFLLDLNS FGDSMKALRN 960
QANACQQQQA APVEGVAGEQ RVMALYDFQA RSPREVTMKK GDVLTLLSSI NKDWWKVEAA 1020
DHQGIVPAVY VRRLAHDEFP MLPQRRREEP GNITQRQEQI ENQYRSLLDR AEERRRRLLQ 1080
RYNEFLLAYE AGDMLEWIQE KKAENTGVEL DDVWELQKKF DEFQKDLNTN EPRLRDINKV 1140
ADDLLFEGLL TPEGAQIRQE LNSRWGSLQR LADEQRQLLG SAHAVEVFHR EADDTKEQIE 1200
KKCQALSAAD PGSDLFSVQA LQRRHEGFER DLVPLGDKVT ILGETAERLS ESHPDATEDL 1260
QRQKMELNEA WEDLQGRTKD RKESLNEAQK FYLFLSKARD LQNWISSIGG MVSSQELAED 1320
LTGIEILLER HQEHRADMEA EAPTFQALED FSAELIDSGH HASPEIEKKL QAVKLERDDL 1380
EKAWEKRKKI LDQCLELQMF QGNCDQVESW MVARENSLRS DDKSSLDSLE ALMKKRDDLD 1440
KAITAQEGKI TDLEHFAESL IADEHYAKEE IATRLQRVLD RWKALKAQLI DERTKLGDYA 1500
NLKQFYRDLE ELEEWISEML PTACDESYKD ATNIQRKYLK HQTFAHEVDG RSEQVHGVIN 1560
LGNSLIECSA CDGNEEAMKE QLEQLKEHWD HLLERTNDKG KKLNEASRQQ RFNTSIRDFE 1620
FWLSEAETLL AMKDQARDLA SAGNLLKKHQ LLEREMLARE DALKDLNTLA EDLLSSGTFN 1680
VDQIVKKKDN VNKRFLNVQE LAAAHHEKLK EAYALFQFFQ DLDDEESWIE EKLIRVSSQD 1740
YGRDLQGVQN LLKKHKRLEG ELVAHEPAIQ NVLDMAEKLK DKAAVGQEEI QLRLAQFVEH 1800
WEKLKELAKA RGLKLEESLE YLQFMQNAEE EEAWINEKNA LAVRGDCGDT LAATQSLLMK 1860
HEALENDFAV HETRVQNVCA QGEDILNKVL QEESQNKEIS SKIEALNEKT PSLAKAIAAW 1920
KLQLEDDYAF QEFNWKADVV EAWIADKETS LKTNGNGADL GDFLTLLAKQ DTLDASLQSF 1980
QQERLPEITD LKDKLISAQH NQSKAIEERY AALLKRWEQL LEASAVHRQK LLEKQLPLQK 2040
AEDLFVEFAH KASALNNWCE KMEENLSEPV HCVSLNEIRQ LQKDHEDFLA SLARAQADFK 2100
CLLELDQQIK ALGVPSSPYT WLTVEVLERT WKHLSDIIEE REQELQKEEA RQVKNFEMCQ 2160
EFEQNASTFL QWILETRAYF LDGSLLKETG TLESQLEANK RKQKEIQAMK RQLTKIVDLG 2220
DNLEDALILD IKYSTIGLAQ QWDQLYQLGL RMQHNLEQQI QAKDIKGVSE ETLKEFSTIY 2280
KHFDENLTGR LTHKEFRSCL RGLNYYLPMV EEDEHEPKFE KFLDAVDPGR KGYVSLEDYT 2340
AFLIDKESEN IKSSDEIENA FQALAEGKSY ITKEDMKQAL TPEQVSFCAT HMQQYMDPRG 2400
RSHLSGYDYV GFTNSYFGN 2419 
Gene Ontology
 GO:0032437; C:cuticular plate; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031235; C:intrinsic to internal side of plasma membrane; TAS:BHF-UCL.
 GO:0008091; C:spectrin; TAS:ProtInc.
 GO:0014731; C:spectrin-associated cytoskeleton; IDA:BHF-UCL.
 GO:0051015; F:actin filament binding; TAS:ProtInc.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0007015; P:actin filament organization; TAS:ProtInc.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0030097; P:hemopoiesis; IEA:Compara.
 GO:0002260; P:lymphocyte homeostasis; IEA:Compara.
 GO:0007009; P:plasma membrane organization; IEA:Compara.
 GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:Compara.
 GO:0032092; P:positive regulation of protein binding; IEA:Compara.
 GO:0042102; P:positive regulation of T cell proliferation; IEA:Compara.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. 
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
 SM00054; EFh
 SM00326; SH3
 SM00150; SPEC 
PROSITE
 PS50222; EF_HAND_2
 PS50002; SH3 
PRINTS
 PR01887; SPECTRNALPHA.