CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039418
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spectrin beta 3 
Protein Synonyms/Alias
 Spectrin beta chain, non-erythrocytic 2 
Gene Name
 Sptbn2 
Gene Synonyms/Alias
 Spnb3; rCG_48072 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
173SVETEDNKEKKSAKDubiquitination[1]
229LLDFESLKKCNAHYNacetylation[2]
358RTVEKPPKFTEKGNLacetylation[2]
404KAWERLEKAEHERELacetylation[2]
1213AADAAIKKLEDFMSTacetylation[2]
1357LKVLVSEKLEDLHRRacetylation[2]
1437REMAVREKEVEAIQAacetylation[2]
1469TSRAVEEKFRALCQPacetylation[2]
1478RALCQPMKDRCRRLQacetylation[2]
1571AELQEMWKRLSHELEacetylation[2]
1674IRQAQVDKLYAGLKEacetylation[2]
1874QKAYAGDKAEEIGRHacetylation[2]
1909LLLDTTDKFRFFKAVacetylation[2]
1987AAEEISEKLSQLQSRacetylation[2]
2259RGSLGFYKDARAASAacetylation[2]
2385EKRFSFFKKNK****acetylation[2]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
  
Sequence Annotation
  
Keyword
 Actin-binding; Complete proteome; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2388 AA 
Protein Sequence
MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA LADEREAVQK 60
KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG ETLPKPTKGR MRIHCLENVD 120
KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLVWTIILRF QIQDISVETE DNKEKKSAKD 180
ALLLWCQMKT AGYPNVNVHN FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA 240
FNLAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA 300
MEAEHLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT 360
EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ 420
EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR 480
VQAVDAVAAE LAAEHYHDIK RIAARQNNVA RLWDFLREMV AARRERLLLN LELQKVFQDL 540
LYLMDWMAEM KGRLQSQDLG KHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCDP 600
GKEYRPCDPQ LVSERVATLE QSYEALCELA ATRRARLEES RRLWRFLWEV GEAEAWVREQ 660
QHLLASAETG RDLTGVLRLL NKHTALRGEM SGRLGPLKLT LEQGQQLVAE GHPGANQAST 720
RAAELQAQWE RLEALAEERA QRLAQAASLY QFQADANDME AWLVDALRLV SSPEVGHDEF 780
STQALARQHR ALEEEIRAHR PTLDALREQA AALPPALSHT PEVQGRVPTL EQHYEELQAR 840
AGERARALEA ALAFYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE 900
MNALAARVTA VSDIAEQLLK ASPPGKDRII GTQEQLNQRW QQFRSLADGK KAALTSALSI 960
QNYHLECTET QAWMREKTKV IESTQDLGND LAGVLALQRK LAGTERDLEA ISARVGELTQ 1020
EANALAAGHP AQAPAINTRL GEVQTGWEDL RATMRRREES LGEARRLQDF LRSLDDFQAW 1080
LGRTQTAVAS EEGPATLPEA EALLAQHAAL RGEVERAQSE YSRLRTLGEE VTRDQADPQC 1140
LFLRQRLEAL GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYVLSHTEM 1200
PGTLQAADAA IKKLEDFMST MDANGERIRG LLEAGRQLVS KGNIHAEKIQ EKADSIEKRH 1260
RKNQEAVQQL LGRLRDNREQ QHFLQDCQEL KLWIDEKMLT AQDVSYDEAR NLHTKWQKHQ 1320
AFMAELAANK DWLDKVDKEG RELTLEKPEL KVLVSEKLED LHRRWDELET TTQAKARSLF 1380
DANRAELFAQ SCSALESWLE SLQAQLHSDD YGKDLTSVNI LLKKQQMLER EMAVREKEVE 1440
AIQAQAKALA QEDQSAGEVE RTSRAVEEKF RALCQPMKDR CRRLQASREQ HQFHRDVEDE 1500
ILWVTERLPM ASSLEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLKER QRTLGTAAAG 1560
PELAELQEMW KRLSHELELR GKRLEEALRA QQFYRDAAEA EAWMGEQELH MMGQEKAKDE 1620
LSAQAEVKKH QVLEQALADY AQTIKQLAAS SQDMIDHEHP ESTRLTIRQA QVDKLYAGLK 1680
ELAGERRERL QEHLRLCQLR RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS 1740
RDTSTIGQER VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA 1800
YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ ALSTQVQQVQ 1860
DDGLRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR QLLLDTTDKF RFFKAVRELM 1920
LWMDGINLQM DAQERPRDVS SADLVIKNQQ GIKAEIEARA DRFSACIDMG QELLARNHYA 1980
AEEISEKLSQ LQSRRQETAE KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE 2040
LGCTVDEVES LIKRHEAFQK SAVAWEERFS ALEKLTALEE RENEQKRKRE EEERRKQPPT 2100
SEPMASQPEG SLVDGQRVLD TAWDGTQSKL PPSTQAPSIN GVCTDTESSQ PLLEQQRLEQ 2160
SNVPEGPGSG TGDESSGPRG ERQTLPRGPA PSPMPQSRSS ESAHVATLPA RGAELSAQEQ 2220
MEGTLCRKQE MEAFNKKAAN RSWQNVYCVL RRGSLGFYKD ARAASAGVPY HGEVPVSLAR 2280
AQGSVAFDYR KRKHVFKLGL QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSASGEPEEP 2340
VVPSASRGLT RAMTMPPVSQ PEGSIVLRSK DGREREREKR FSFFKKNK 2388 
Gene Ontology
 GO:0008091; C:spectrin; IEA:InterPro.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. 
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.