CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000347
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spectrin beta chain, non-erythrocytic 2 
Protein Synonyms/Alias
 Beta-III spectrin; Spinocerebellar ataxia 5 protein 
Gene Name
 SPTBN2 
Gene Synonyms/Alias
 KIAA0302; SCA5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
65VQKKTFTKWVNSHLAubiquitination[1, 2]
121HCLENVDKALQFLKEubiquitination[2]
217AFNAIVHKHRPDLLDacetylation[3]
291KALAVEGKRIGKVLDubiquitination[2]
2053DEVESLIKRHEAFQKubiquitination[2]
2074ERFCALEKLTALEERubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224] 
Functional Description
 Probably plays an important role in neuronal membrane skeleton. 
Sequence Annotation
 DOMAIN 1 278 Actin-binding.
 DOMAIN 57 161 CH 1.
 DOMAIN 176 278 CH 2.
 REPEAT 305 415 Spectrin 1.
 REPEAT 425 529 Spectrin 2.
 REPEAT 531 639 Spectrin 3.
 REPEAT 641 745 Spectrin 4.
 REPEAT 747 850 Spectrin 5.
 REPEAT 852 956 Spectrin 6.
 REPEAT 958 1063 Spectrin 7.
 REPEAT 1065 1170 Spectrin 8.
 REPEAT 1172 1276 Spectrin 9.
 REPEAT 1278 1381 Spectrin 10.
 REPEAT 1383 1486 Spectrin 11.
 REPEAT 1488 1586 Spectrin 12.
 REPEAT 1588 1692 Spectrin 13.
 REPEAT 1694 1799 Spectrin 14.
 REPEAT 1801 1905 Spectrin 15.
 REPEAT 1907 2011 Spectrin 16.
 REPEAT 2013 2075 Spectrin 17.
 DOMAIN 2218 2328 PH.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2171 2171 Phosphoserine.
 MOD_RES 2359 2359 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Actin capping; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Neurodegeneration; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Spinocerebellar ataxia. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2390 AA 
Protein Sequence
MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA LADEREAVQK 60
KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG EILPKPTKGR MRIHCLENVD 120
KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLVWTIILRF QIQDISVETE DNKEKKSAKD 180
ALLLWCQMKT AGYPNVNVHN FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA 240
FNLAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA 300
MEAERLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT 360
EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ 420
EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR 480
VQAVDAVAAE LAAERYHDIK RIAARQHNVA RLWDFLRQMV AARRERLLLN LELQKVFQDL 540
LYLMDWMEEM KGRLQSQDLG RHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCNP 600
GKEYRPCDPQ LVSERVAKLE QSYEALCELA AARRARLEES RRLWRFLWEV GEAEAWVREQ 660
QHLLASADTG RDLTGALRLL NKHTALRGEM SGRLGPLKLT LEQGQQLVAE GHPGASQASA 720
RAAELQAQWE RLEALAEERA QRLAQAASLY QFQADANDME AWLVDALRLV SSPELGHDEF 780
STQALARQHR ALEEEIRSHR PTLDALREQA AALPPTLSRT PEVQSRVPTL ERHYEELQAR 840
AGERARALEA ALALYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE 900
MNTLAAQITA VNDIAEQLLK ANPPGKDRIV NTQEQLNHRW QQFRRLADGK KAALTSALSI 960
QNYHLECTET QAWMREKTKV IESTQGLGND LAGVLALQRK LAGTERDLEA IAARVGELTR 1020
EANALAAGHP AQAVAINARL REVQTGWEDL RATMRRREES LGEARRLQDF LRSLDDFQAW 1080
LGRTQTAVAS EEGPATLPEA EALLAQHAAL RGEVERAQSE YSRLRALGEE VTRDQADPQC 1140
LFLRQRLEAL GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYVLSHTEM 1200
PGTLQAADAA IKKLEDFMST MDANGERIHG LLEAGRQLVS EGNIHADKIR EKADSIERRH 1260
KKNQDAAQQF LGRLRDNREQ QHFLQDCHEL KLWIDEKMLT AQDVSYDEAR NLHTKWQKHQ 1320
AFMAELAANK DWLDKVDKEG RELTLEKPEL KALVSEKLRD LHRRWDELET TTQAKARSLF 1380
DANRAELFAQ SCCALESWLE SLQAQLHSDD YGKDLTSVNI LLKKQQMLEW EMAVREKEVE 1440
AIQAQAKALA QEDQGAGEVE RTSRAVEEKF RALCQPMRER CRRLQASREQ HQFHRDVEDE 1500
ILWVTERLPM ASSMEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLRER QRALGAAAAG 1560
PELAELQEMW KRLGHELELR GKRLEDALRA QQFYRDAAEA EAWMGEQELH MMGQEKAKDE 1620
LSAQAEVKKH QVLEQALADY AQTIHQLAAS SQDMIDHEHP ESTRISIRQA QVDKLYAGLK 1680
ELAGERRERL QEHLRLCQLR RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS 1740
RDTSTIGQER VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA 1800
YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ ALSPQVQQVQ 1860
DDGHRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR QLLLDTTDKF RFFKAVRELM 1920
LWMDEVNLQM DAQERPRDVS SADLVIKNQQ GIKAEIEARA DRFSSCIDMG KELLARSHYA 1980
AEEISEKLSQ LQARRQETAE KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE 2040
LGCTVDEVES LIKRHEAFQK SAVAWEERFC ALEKLTALEE REKERKRKRE EEERRKQPPA 2100
PEPTASVPPG DLVGGQTASD TTWDGTQPRP PPSTQAPSVN GVCTDGEPSQ PLLGQQRLEH 2160
SSFPEGPGPG SGDEANGPRG ERQTRTRGPA PSAMPQSRST ESAHAATLPP RGPEPSAQEQ 2220
MEGMLCRKQE MEAFGKKAAN RSWQNVYCVL RRGSLGFYKD AKAASAGVPY HGEVPVSLAR 2280
AQGSVAFDYR KRKHVFKLGL QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSASGEPEEP 2340
VVPSTTRGMT RAMTMPPVSP VGAEGPVVLR SKDGRERERE KRFSFFKKNK 2390 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0008091; C:spectrin; IDA:UniProtKB.
 GO:0003779; F:actin binding; TAS:ProtInc.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0030534; P:adult behavior; IEA:Compara.
 GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0021692; P:cerebellar Purkinje cell layer morphogenesis; IEA:Compara.
 GO:0035264; P:multicellular organism growth; IEA:Compara.
 GO:0007416; P:synapse assembly; IEA:Compara.
 GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB. 
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.