CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014415
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
2138SQTYQNYKNFNSRRTubiquitination[1]
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] 
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
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 MDEMKVLLLS 540
QDYGKHLLGV EDLLQKHALV EADIAIQAER VRGVNASAQK FATDGEGYKP CDPQVIRDRV 600
AHMEFCYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW IREKEKILSS DDYGKDLTSV 660
MRLLSKHRAF EDEMSGRSGH FEQAIKEGED MIAEEHFGSE KIRERIIYIR EQWANLEQLS 720
AIRKKRLEEA SLLHQFQADA DDIDAWMLDI LKIVSSNDVG HDEYSTQSLV KKHKDVAEEI 780
TNYRPTIDTL HEQASALPQA HAESPDVKGR LAGIEERCKE MAELTRLRKQ ALQDTLALYK 840
MFSEADACEL WIDEKEQWLN NMQIPEKLED LEVIQHRFES LEPEMNNQAS RVAVVNQIAR 900
QLMHNGHPSE KEIRAQQDKL 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 DDRHRKNREA 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 LSERKHNLLA SKEIHQFNRD VEDEILWVGE RMPLATSTDH 1500
GHNLQTVQLL IKKNQTLQKE IQGHQPRIDD IFERSQNIIT DSSSLNAEAI RQRLADLKQL 1560
WGLLIEETEK RHRRLEEAHK AQQYYFDAAE AEAWMSEQEL YMMSEEKAKD EQSAVSMLKK 1620
HQILEQAVED YAETVHQLSK TSRALVADSH PESERISMRQ SKVDKLYAGL KDLAEERRGK 1680
LDERHRLFQL NREVDDLEQW IAEREVVAGS HELGQDYEHV TMLQERFREF ARDTGNIGQE 1740
RVDTVNNMAD ELINSGHSDA ATIAEWKDGL NEAWADLLEL IDTRTQILAA SYELHKFYHD 1800
AKEIFGRIQD KHKKLPEELG RDQNTVETLQ RMHTTFEHDI QALGTQVRQL QEDAARLQAA 1860
YAGDKADDIQ KRENEVLEAW KSLLDACEGR RVRLVDTGDK FRFFSMVRDL MLWMEDVIRQ 1920
IEAQEKPRDV SSVELLMNNH QGIKAEIDAR NDSFTACIEL GKSLLARKHY ASEEIKEKLL 1980
QLTEKRKEMI DKWEDRWEWL RLILEVHQFS RDASVAEAWL LGQEPYLSSR EIGQSVDEVE 2040
KLIKRHEAFE KSAATWDERF SALERLTTLE LLEVRRQQEE EERKRRPPSP DPNTKVSEEA 2100
ESQQWDTSKG DQVSQNGLPA EQGSPRVSYR SQTYQNYKNF NSRRTASDHS WSGM 2154 
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.