CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014414
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spectrin beta chain, non-erythrocytic 1 
Protein Synonyms/Alias
 Beta-II spectrin; Embryonic liver fodrin; Fodrin beta chain 
Gene Name
 Sptbn1 
Gene Synonyms/Alias
 Elf; Spnb-2; Spnb2; Sptb2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
57DEREAVQKKTFTKWVubiquitination[1]
62VQKKTFTKWVNSHLAubiquitination[1]
90RDGRMLIKLLEVLSGacetylation[2]
90RDGRMLIKLLEVLSGubiquitination[1]
102LSGERLPKPTKGRMRubiquitination[1]
105ERLPKPTKGRMRIHCubiquitination[1]
118HCLENVDKALQFLKEubiquitination[1]
124DKALQFLKEQRVHLEubiquitination[1]
170SVETEDNKEKKSAKDubiquitination[1]
359KPPKFTEKGNLEVLLubiquitination[1]
430LARRFDRKAAMRETWubiquitination[1]
558LLSQDYGKHLLGVEDacetylation[2]
558LLSQDYGKHLLGVEDubiquitination[1]
593GVNASAQKFATDGEGacetylation[2]
593GVNASAQKFATDGEGubiquitination[1]
602ATDGEGYKPCDPQVIacetylation[2]
659GWIREKEKILSSDDYubiquitination[1]
668LSSDDYGKDLTSVMRubiquitination[1]
842AELTRLRKQALQDTLubiquitination[1]
924HNGHPSEKEIRAQQDubiquitination[1]
976SWIREKTKVIESTQDubiquitination[1]
1011DLVAIEAKLSDLQKEubiquitination[1]
1017AKLSDLQKEAEKLESubiquitination[1]
1063ASLGEASKLQQFLRDubiquitination[1]
1108LTQHENIKNEIDNYEacetylation[2]
1335EWLDKIEKEGMQLISubiquitination[1]
1360EKLTGLHKMWEVLESubiquitination[1]
1381QRLFDANKAELFTQSubiquitination[1]
1420TSVNILLKKQQMLENubiquitination[1]
1421SVNILLKKQQMLENQubiquitination[1]
1622MMSEEKAKDEQSAVSubiquitination[1]
1633SAVSMLKKHQILEQAacetylation[2]
1653ETVHQLSKTSRALVAacetylation[2]
1678MRQSKVDKLYAGLKDubiquitination[1]
1684DKLYAGLKDLAEERRubiquitination[1]
1815HKFYHDAKEIFGRIQacetylation[3]
1815HKFYHDAKEIFGRIQubiquitination[1]
1878QAAYAGDKADDIQKRacetylation[4]
1913RLVDTGDKFRFFSMVacetylation[2]
2054QSVDEVEKLIKRHEAubiquitination[1]
2176PTLDRKAKSALPAQSubiquitination[1]
2240MGFYKDAKSAASGIPubiquitination[1]
2268CEVALDYKKKKHVFKacetylation[4]
2343TSESSPGKREKDKEKubiquitination[1]
2361KRFSLFGKKK*****acetylation[2]
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] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 1 275 Actin-binding.
 DOMAIN 54 158 CH 1.
 DOMAIN 173 275 CH 2.
 REPEAT 276 384 Spectrin 1.
 REPEAT 385 498 Spectrin 2.
 REPEAT 499 608 Spectrin 3.
 REPEAT 609 714 Spectrin 4.
 REPEAT 715 819 Spectrin 5.
 REPEAT 820 925 Spectrin 6.
 REPEAT 926 1032 Spectrin 7.
 REPEAT 1033 1139 Spectrin 8.
 REPEAT 1140 1245 Spectrin 9.
 REPEAT 1246 1350 Spectrin 10.
 REPEAT 1351 1462 Spectrin 11.
 REPEAT 1463 1562 Spectrin 12.
 REPEAT 1563 1668 Spectrin 13.
 REPEAT 1669 1775 Spectrin 14.
 REPEAT 1776 1881 Spectrin 15.
 REPEAT 1882 1987 Spectrin 16.
 REPEAT 1988 2132 Spectrin 17.
 DOMAIN 2196 2306 PH.
 REGION 1563 2093 Interaction with ANK2 (By similarity).
 MOD_RES 2 2 N-acetylthreonine (By similarity).
 MOD_RES 90 90 N6-acetyllysine (By similarity).
 MOD_RES 257 257 Phosphoserine.
 MOD_RES 817 817 Phosphoserine (By similarity).
 MOD_RES 999 999 Phosphothreonine.
 MOD_RES 1057 1057 Phosphoserine (By similarity).
 MOD_RES 1447 1447 Phosphoserine (By similarity).
 MOD_RES 1805 1805 Phosphotyrosine.
 MOD_RES 1815 1815 N6-acetyllysine (By similarity).
 MOD_RES 1913 1913 N6-acetyllysine (By similarity).
 MOD_RES 1918 1918 Phosphoserine.
 MOD_RES 1989 1989 N6-acetyllysine (By similarity).
 MOD_RES 2102 2102 Phosphoserine.
 MOD_RES 2115 2115 Phosphoserine.
 MOD_RES 2127 2127 Phosphoserine.
 MOD_RES 2137 2137 Phosphoserine.
 MOD_RES 2159 2159 Phosphoserine (By similarity).
 MOD_RES 2160 2160 Phosphoserine (By similarity).
 MOD_RES 2163 2163 Phosphoserine (By similarity).
 MOD_RES 2164 2164 Phosphoserine.
 MOD_RES 2168 2168 Phosphoserine.
 MOD_RES 2186 2186 Phosphothreonine (By similarity).
 MOD_RES 2194 2194 Phosphothreonine.
 MOD_RES 2318 2318 Phosphoserine (By similarity).
 MOD_RES 2319 2319 Phosphothreonine (By similarity).
 MOD_RES 2327 2327 Phosphothreonine.
 MOD_RES 2339 2339 Phosphoserine (By similarity).
 MOD_RES 2340 2340 Phosphoserine (By similarity).
 MOD_RES 2357 2357 Phosphoserine.
 CARBOHYD 2323 2323 O-linked (GlcNAc).  
Keyword
 3D-structure; Acetylation; Actin capping; Actin-binding; Alternative splicing; Calmodulin-binding; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2363 AA 
Protein Sequence
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF 60
TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL 120
QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL 180
LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL 240
AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET 300
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG 360
NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL 420
EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA 480
VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI 540
MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG 600
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI 660
LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII 720
YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ 780
SLVKKHKDVA EEITNYRPTI DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL 840
RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN 900
QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY 960
HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE 1020
KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR 1080
TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL 1140
RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT 1200
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN 1260
REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM 1320
AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN 1380
KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ 1440
SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW 1500
VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IITDSSSLNA 1560
EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD AAEAEAWMSE QELYMMSEEK 1620
AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY 1680
AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF 1740
REFARDTGNI GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI 1800
LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV 1860
RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC EGRRVRLVDT GDKFRFFSMV 1920
RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTAC IELGKSLLAR 1980
KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL 2040
SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP 2100
PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV NGAAEQRTSS 2160
KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME GFLNRKHEWE AHNKKASSRS 2220
WHNVYCVINN QEMGFYKDAK SAASGIPYHS EVPVSLKEAI CEVALDYKKK KHVFKLRLSD 2280
GNEYLFQAKD DEEMNTWIQA ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS 2340
PGKREKDKEK DKEKRFSLFG KKK 2363 
Gene Ontology
 GO:0030673; C:axolemma; IDA:BHF-UCL.
 GO:0032437; C:cuticular plate; IDA:MGI.
 GO:0031430; C:M band; IDA:BHF-UCL.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0008091; C:spectrin; IEA:InterPro.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:Compara.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:MGI.
 GO:0043001; P:Golgi to plasma membrane protein transport; IEA:Compara.
 GO:0071709; P:membrane assembly; IEA:Compara.
 GO:0000281; P:mitotic cytokinesis; IEA:Compara.
 GO:0072661; P:protein targeting to plasma membrane; IMP:BHF-UCL.
 GO:0007184; P:SMAD protein import into nucleus; IDA:MGI. 
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.