CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010820
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Spectrin beta chain, non-erythrocytic 1 
Protein Synonyms/Alias
 Beta-II spectrin; Fodrin beta chain; Spectrin, non-erythroid beta chain 1 
Gene Name
 SPTBN1 
Gene Synonyms/Alias
 SPTB2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33NQLEGRFKQLQDEREubiquitination[1]
49VQKKTFTKWVNSHLAubiquitination[2]
580GVNASAQKFATDGEGubiquitination[2]
646GWIREKEKILSSDDYubiquitination[2]
819SGIEERYKEVAELTRubiquitination[2]
1322EWLDKIEKEGMQLISubiquitination[2]
1347EKLTGLHKMWEVLESubiquitination[2]
1665MRQSKVDKLYAGLKDubiquitination[2]
Reference
 [1] 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]
 [2] 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] 
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 2133 Spectrin 17.
 DOMAIN 2197 2307 PH.
 REGION 1563 2093 Interaction with ANK2.
 MOD_RES 2 2 N-acetylthreonine.
 MOD_RES 90 90 N6-acetyllysine.
 MOD_RES 257 257 Phosphoserine (By similarity).
 MOD_RES 817 817 Phosphoserine.
 MOD_RES 825 825 Phosphoserine.
 MOD_RES 999 999 Phosphothreonine (By similarity).
 MOD_RES 1057 1057 Phosphoserine.
 MOD_RES 1447 1447 Phosphoserine.
 MOD_RES 1805 1805 Phosphotyrosine (By similarity).
 MOD_RES 1815 1815 N6-acetyllysine.
 MOD_RES 1913 1913 N6-acetyllysine.
 MOD_RES 1918 1918 Phosphoserine (By similarity).
 MOD_RES 1989 1989 N6-acetyllysine.
 MOD_RES 2102 2102 Phosphoserine.
 MOD_RES 2128 2128 Phosphoserine.
 MOD_RES 2138 2138 Phosphoserine.
 MOD_RES 2160 2160 Phosphoserine.
 MOD_RES 2161 2161 Phosphoserine.
 MOD_RES 2164 2164 Phosphoserine.
 MOD_RES 2165 2165 Phosphoserine.
 MOD_RES 2169 2169 Phosphoserine.
 MOD_RES 2187 2187 Phosphothreonine.
 MOD_RES 2195 2195 Phosphothreonine (By similarity).
 MOD_RES 2319 2319 Phosphoserine.
 MOD_RES 2320 2320 Phosphothreonine.
 MOD_RES 2328 2328 Phosphothreonine.
 MOD_RES 2340 2340 Phosphoserine.
 MOD_RES 2341 2341 Phosphoserine.
 MOD_RES 2358 2358 Phosphoserine (By similarity).
 CARBOHYD 2324 2324 O-linked (GlcNAc) (By similarity).  
Keyword
 3D-structure; Acetylation; Actin capping; Actin-binding; Alternative splicing; Calmodulin-binding; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2364 AA 
Protein Sequence
MELQRTSSIS GPLSPAYTGQ VPYNYNQLEG RFKQLQDERE AVQKKTFTKW VNSHLARVSC 60
RITDLYTDLR DGRMLIKLLE VLSGERLPKP TKGRMRIHCL ENVDKALQFL KEQRVHLENM 120
GSHDIVDGNH RLTLGLIWTI ILRFQIQDIS VETEDNKEKK SAKDALLLWC QMKTAGYPNV 180
NIHNFTTSWR DGMAFNALIH KHRPDLIDFD KLKKSNAHYN LQNAFNLAEQ HLGLTKLLDP 240
EDISVDHPDE KSIITYVVTY YHYFSKMKAL AVEGKRIGKV LDNAIETEKM IEKYESLASD 300
LLEWIEQTII ILNNRKFANS LVGVQQQLQA FNTYRTVEKP PKFTEKGNLE VLLFTIQSKM 360
RANNQKVYMP REGKLISDIN KAWERLEKAE HERELALRNE LIRQEKLEQL ARRFDRKAAM 420
RETWLSENQR LVSQDNFGFD LPAVEAATKK HEAIETDIAA YEERVQAVVA VARELEAENY 480
HDIKRITARK DNVIRLWEYL LELLRARRQR LEMNLGLQKI FQEMLYIMDW MDEMKVLVLS 540
QDYGKHLLGV EDLLQKHTLV EADIGIQAER VRGVNASAQK FATDGEGYKP CDPQVIRDRV 600
AHMEFCYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW IREKEKILSS DDYGKDLTSV 660
MRLLSKHRAF EDEMSGRSGH FEQAIKEGED MIAEEHFGSE KIRERIIYIR EQWANLEQLS 720
AIRKKRLEEA SLLHQFQADA DDIDAWMLDI LKIVSSSDVG HDEYSTQSLV KKHKDVAEEI 780
ANYRPTLDTL HEQASALPQE HAESPDVRGR LSGIEERYKE VAELTRLRKQ ALQDTLALYK 840
MFSEADACEL WIDEKEQWLN NMQIPEKLED LEVIQHRFES LEPEMNNQAS RVAVVNQIAR 900
QLMHSGHPSE KEIKAQQDKL NTRWSQFREL VDRKKDALLS ALSIQNYHLE CNETKSWIRE 960
KTKVIESTQD LGNDLAGVMA LQRKLTGMER DLVAIEAKLS DLQKEAEKLE SEHPDQAQAI 1020
LSRLAEISDV WEEMKTTLKN REASLGEASK LQQFLRDLDD FQSWLSRTQT AIASEDMPNT 1080
LTEAEKLLTQ HENIKNEIDN YEEDYQKMRD MGEMVTQGQT DAQYMFLRQR LQALDTGWNE 1140
LHKMWENRQN LLSQSHAYQQ FLRDTKQAEA FLNNQEYVLA HTEMPTTLEG AEAAIKKQED 1200
FMTTMDANEE KINAVVETGR RLVSDGNINS DRIQEKVDSI DDRHRKNRET ASELLMRLKD 1260
NRDLQKFLQD CQELSLWINE KMLTAQDMSY DEARNLHSKW LKHQAFMAEL ASNKEWLDKI 1320
EKEGMQLISE KPETEAVVKE KLTGLHKMWE VLESTTQTKA QRLFDANKAE LFTQSCADLD 1380
KWLHGLESQI QSDDYGKDLT SVNILLKKQQ MLENQMEVRK KEIEELQSQA QALSQEGKST 1440
DEVDSKRLTV QTKFMELLEP LNERKHNLLA SKEIHQFNRD VEDEILWVGE RMPLATSTDH 1500
GHNLQTVQLL IKKNQTLQKE IQGHQPRIDD IFERSQNIVT DSSSLSAEAI RQRLADLKQL 1560
WGLLIEETEK RHRRLEEAHR AQQYYFDAAE AEAWMSEQEL YMMSEEKAKD EQSAVSMLKK 1620
HQILEQAVED YAETVHQLSK TSRALVADSH PESERISMRQ SKVDKLYAGL KDLAEERRGK 1680
LDERHRLFQL NREVDDLEQW IAEREVVAGS HELGQDYEHV TMLQERFREF ARDTGNIGQE 1740
RVDTVNHLAD ELINSGHSDA ATIAEWKDGL NEAWADLLEL IDTRTQILAA SYELHKFYHD 1800
AKEIFGRIQD KHKKLPEELG RDQNTVETLQ RMHTTFEHDI QALGTQVRQL QEDAARLQAA 1860
YAGDKADDIQ KRENEVLEAW KSLLDACESR RVRLVDTGDK FRFFSMVRDL MLWMEDVIRQ 1920
IEAQEKPRDV SSVELLMNNH QGIKAEIDAR NDSFTTCIEL GKSLLARKHY ASEEIKEKLL 1980
QLTEKRKEMI DKWEDRWEWL RLILEVHQFS RDASVAEAWL LGQEPYLSSR EIGQSVDEVE 2040
KLIKRHEAFE KSAATWDERF SALERLTTLE LLEVRRQQEE EERKRRPPSP EPSTKVSEEA 2100
ESQQQWDTSK GEQVSQNGLP AEQGSPRVSY RSQTYQNYKN FNSRRTASDQ PWSGL 2155 
Gene Ontology
 GO:0030673; C:axolemma; ISS:BHF-UCL.
 GO:0032437; C:cuticular plate; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031430; C:M band; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HGNC.
 GO:0008091; C:spectrin; TAS:ProtInc.
 GO:0014731; C:spectrin-associated cytoskeleton; NAS:BHF-UCL.
 GO:0003779; F:actin binding; TAS:ProtInc.
 GO:0030506; F:ankyrin binding; NAS:BHF-UCL.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005200; F:structural constituent of cytoskeleton; IMP:BHF-UCL.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007182; P:common-partner SMAD protein phosphorylation; IEA:Compara.
 GO:0043001; P:Golgi to plasma membrane protein transport; IMP:BHF-UCL.
 GO:0071709; P:membrane assembly; IMP:BHF-UCL.
 GO:0000281; P:mitotic cytokinesis; IMP:BHF-UCL.
 GO:0072661; P:protein targeting to plasma membrane; IMP:BHF-UCL.
 GO:0007184; P:SMAD protein import into nucleus; IEA:Compara. 
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.