CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003903
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spectrin beta chain, erythrocytic 
Protein Synonyms/Alias
 Beta-I spectrin 
Gene Name
 SPTB 
Gene Synonyms/Alias
 SPTB1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
124DKALQFLKEQRVHLEacetylation[1]
224PDLIDFDKLKDSNARacetylation[1]
462AAVEAAKKKHEAIETglycation[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] ATP-dependent mechanism protects spectrin against glycation in human erythrocytes.
 Manno S, Mohandas N, Takakuwa Y.
 J Biol Chem. 2010 Oct 29;285(44):33923-9. [PMID: 20724481] 
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
 DOMAIN 2 275 Actin-binding.
 DOMAIN 54 158 CH 1.
 DOMAIN 173 275 CH 2.
 REPEAT 276 384 Spectrin 1.
 REPEAT 385 498 Spectrin 2.
 REPEAT 499 607 Spectrin 3.
 REPEAT 608 713 Spectrin 4.
 REPEAT 714 818 Spectrin 5.
 REPEAT 819 924 Spectrin 6.
 REPEAT 925 1031 Spectrin 7.
 REPEAT 1032 1138 Spectrin 8.
 REPEAT 1139 1244 Spectrin 9.
 REPEAT 1245 1349 Spectrin 10.
 REPEAT 1350 1455 Spectrin 11.
 REPEAT 1456 1554 Spectrin 12.
 REPEAT 1555 1660 Spectrin 13.
 REPEAT 1661 1767 Spectrin 14.
 REPEAT 1768 1873 Spectrin 15.
 REPEAT 1874 1979 Spectrin 16.
 REPEAT 1980 2085 Spectrin 17.
 MOD_RES 36 36 Phosphoserine (By similarity).
 MOD_RES 2110 2110 Phosphothreonine.
 MOD_RES 2114 2114 Phosphoserine.
 MOD_RES 2117 2117 Phosphoserine.
 MOD_RES 2123 2123 Phosphoserine.
 MOD_RES 2125 2125 Phosphoserine.
 MOD_RES 2128 2128 Phosphoserine.  
Keyword
 3D-structure; Actin capping; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Elliptocytosis; Hereditary hemolytic anemia; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2137 AA 
Protein Sequence
MTSATEFENV GNQPPYSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF 60
TKWVNSHLAR VSCRITDLYK DLRDGRMLIK LLEVLSGEML PKPTKGKMRI HCLENVDKAL 120
QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVQTQEGR ETRSAKDALL 180
LWCQMKTAGY PHVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFNV 240
AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET 300
EKMIEKYSGL ASDLLTWIEQ TITVLNSRKF ANSLTGVQQQ LQAFSTYRTV EKPPKFQEKG 360
NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYRRELAL RNELIRQEKL 420
EQLARRFDRK AAMRETWLSE NQRLVAQDNF GYDLAAVEAA KKKHEAIETD TAAYEERVRA 480
LEDLAQELEK ENYHDQKRIT ARKDNILRLW SYLQELLQSR RQRLETTLAL QKLFQDMLHS 540
IDWMDEIKAH LLSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVKAITAA TLKFTEGKGY 600
QPCDPQVIQD RISHLEQCFE ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE SWIKEKEQIY 660
SSLDYGKDLT SVLILQRKHK AFEDELRGLD AHLEQIFQEA HGMVARKQFG HPQIEARIKE 720
VSAQWDQLKD LAAFCKKNLQ DAENFFQFQG DADDLKAWLQ DAHRLLSGED VGQDEGATRA 780
LGKKHKDFLE ELEESRGVME HLEQQAQGFP EEFRDSPDVT HRLQALRELY QQVVAQADLR 840
QQRLQEALDL YTVFGETDAC ELWMGEKEKW LAEMEMPDTL EDLEVVQHRF DILDQEMKTL 900
MTQIDGVNLA ANSLVESGHP RSREVKQYQD HLNTRWQAFQ TLVSERREAV DSALRVHNYC 960
VDCEETSKWI TDKTKVVEST KDLGRDLAGI IAIQRKLSGL ERDVAAIQAR VDALERESQQ 1020
LMDSHPEQKE DIGQRQKHLE ELWQGLQQSL QGQEDLLGEV SQLQAFLQDL DDFQAWLSIT 1080
QKAVASEDMP ESLPEAEQLL QQHAGIKDEI DGHQDSYQRV KESGEKVIQG QTDPEYLLLG 1140
QRLEGLDTGW NALGRMWESR SHTLAQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL 1200
EAAEAGIRKF EDFLGSMENN RDKVLSPVDS GNKLVAEGNL YSDKIKEKVQ LIEDRHRKNN 1260
EKAQEASVLL RDNLELQNFL QNCQELTLWI NDKLLTSQDV SYDEARNLHN KWLKHQAFVA 1320
ELASHEGWLE NIDAEGKQLM DEKPQFTALV SQKLEALHRL WDELQATTKE KTQHLSAARS 1380
SDLRLQTHAD LNKWISAMED QLRSDDPGKD LTSVNRMLAK LKRVEDQVNV RKEELGELFA 1440
QVPSMGEEGG DADLSIEKRF LDLLEPLGRR KKQLESSRAK LQISRDLEDE TLWVEERLPL 1500
AQSADYGTNL QTVQLFMKKN QTLQNEILGH TPRVEDVLQR GQQLVEAAEI DCQDLEERLG 1560
HLQSSWDRLR EAAAGRLQRL RDANEAQQYY LDADEAEAWI GEQELYVISD EIPKDEEGAI 1620
VMLKRHLRQQ RAVEDYGRNI KQLASRAQGL LSAGHPEGEQ IIRLQGQVDK HYAGLKDVAE 1680
ERKRKLENMY HLFQLKRETD DLEQWISEKE LVASSPEMGQ DFDHVTLLRD KFRDFARETG 1740
AIGQERVDNV NAFIERLIDA GHSEAATIAE WKDGLNEMWA DLLELIDTRM QLLAASYDLH 1800
RYFYTGAEIL GLIDEKHREL PEDVGLDAST AESFHRVHTA FERELHLLGV QVQQFQDVAT 1860
RLQTAYAGEK AEAIQNKEQE VSAAWQALLD ACAGRRTQLV DTADKFRFFS MARDLLSWME 1920
SIIRQIETQE RPRDVSSVEL LMKYHQGINA EIETRSKNFS ACLELGESLL QRQHQASEEI 1980
REKLQQVMSR RKEMNEKWEA RWERLRMLLE VCQFSRDASV AEAWLIAQEP YLASGDFGHT 2040
VDSVEKLIKR HEAFEKSTAS WAERFAALEK PTTLELKERQ IAERPAEETG PQEEEGETAG 2100
EAPVSHHAAT ERTSPVSLWS RLSSSWESLQ PEPSHPY 2137 
Gene Ontology
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031235; C:intrinsic to internal side of plasma membrane; TAS:BHF-UCL.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0008091; C:spectrin; TAS:ProtInc.
 GO:0014731; C:spectrin-associated cytoskeleton; IDA:BHF-UCL.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0030097; P:hemopoiesis; IEA:Compara.
 GO:0007009; P:plasma membrane organization; IEA:Compara.
 GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:Compara. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR018159; Spectrin/alpha-actinin.
 IPR016343; Spectrin_bsu.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH 
PRINTS