CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010856
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ankyrin-2 
Protein Synonyms/Alias
 ANK-2; Ankyrin-B; Brain ankyrin; Non-erythroid ankyrin 
Gene Name
 ANK2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
118EVVKVLVKEGANINAubiquitination[1]
223HNADVQSKMMVNRTTubiquitination[1]
275TPLHVASKRGNTNMVubiquitination[1]
407TPLHIACKKNRIKVMubiquitination[1]
572TPLHVAAKYGSLDVAubiquitination[1]
802NTALAIAKRLGYISVubiquitination[1]
1213VKKILGNKATFSPIVubiquitination[1]
1416NRLPLFVKVRDTTQEubiquitination[1]
2051KTENQTIKRGQRLPVacetylation[2]
3618DQSHALLKYWLERDGubiquitination[3, 4]
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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions (By similarity). Attaches integral membrane proteins to cytoskeletal elements. Also binds to cytoskeletal proteins. Required for coordinate assembly of Na/Ca exchanger, Na/K ATPase and InsP3 receptor at sarcoplasmic reticulum sites in cardiomyocytes. Required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) in the inner segment of rod photoreceptors. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate. 
Sequence Annotation
 REPEAT 30 62 ANK 1.
 REPEAT 63 92 ANK 2.
 REPEAT 96 125 ANK 3.
 REPEAT 129 158 ANK 4.
 REPEAT 162 191 ANK 5.
 REPEAT 193 220 ANK 6.
 REPEAT 232 261 ANK 7.
 REPEAT 265 294 ANK 8.
 REPEAT 298 327 ANK 9.
 REPEAT 331 360 ANK 10.
 REPEAT 364 393 ANK 11.
 REPEAT 397 426 ANK 12.
 REPEAT 430 459 ANK 13.
 REPEAT 463 492 ANK 14.
 REPEAT 496 525 ANK 15.
 REPEAT 529 558 ANK 16.
 REPEAT 562 591 ANK 17.
 REPEAT 595 624 ANK 18.
 REPEAT 628 657 ANK 19.
 REPEAT 661 690 ANK 20.
 REPEAT 694 723 ANK 21.
 REPEAT 727 756 ANK 22.
 REPEAT 760 789 ANK 23.
 REPEAT 793 822 ANK 24.
 DOMAIN 966 1124 ZU5 1.
 DOMAIN 1125 1288 ZU5 2.
 DOMAIN 1450 1535 Death 1.
 REPEAT 1806 1817 Repeat A.
 REPEAT 1818 1829 Repeat A.
 REPEAT 1830 1841 Repeat A.
 REPEAT 1842 1853 Repeat A.
 REPEAT 1854 1865 Repeat A.
 REPEAT 1866 1877 Repeat A.
 REPEAT 1878 1889 Repeat A.
 REPEAT 1890 1900 Repeat A; approximate.
 REPEAT 1901 1912 Repeat A.
 REPEAT 1913 1924 Repeat A.
 REPEAT 1925 1935 Repeat A; approximate.
 REPEAT 1936 1947 Repeat A.
 REPEAT 1948 1959 Repeat A.
 REPEAT 1960 1971 Repeat A.
 REPEAT 1972 1983 Repeat A.
 DOMAIN 3569 3653 Death 2.
 REGION 966 1125 Interaction with SPTBN1.
 REGION 1289 1423 UPA domain.
 REGION 1806 1983 Repeat-rich region.
 MOD_RES 31 31 Phosphoserine (By similarity).
 MOD_RES 34 34 Phosphoserine (By similarity).
 MOD_RES 378 378 Phosphotyrosine (By similarity).
 MOD_RES 531 531 Phosphotyrosine (By similarity).
 MOD_RES 846 846 Phosphoserine (By similarity).
 MOD_RES 898 898 Phosphoserine (By similarity).
 MOD_RES 1382 1382 Phosphotyrosine (By similarity).
 MOD_RES 1461 1461 Phosphoserine (By similarity).
 MOD_RES 3093 3093 Phosphothreonine (By similarity).
 MOD_RES 3273 3273 Phosphoserine (By similarity).
 MOD_RES 3362 3362 Phosphoserine (By similarity).
 MOD_RES 3390 3390 Phosphoserine (By similarity).
 MOD_RES 3409 3409 Phosphoserine (By similarity).
 MOD_RES 3410 3410 Phosphotyrosine (By similarity).
 MOD_RES 3735 3735 Phosphoserine (By similarity).
 MOD_RES 3776 3776 Phosphothreonine (By similarity).
 MOD_RES 3802 3802 Phosphoserine (By similarity).
 MOD_RES 3803 3803 Phosphothreonine (By similarity).
 MOD_RES 3823 3823 Phosphoserine (By similarity).
 MOD_RES 3844 3844 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Alternative splicing; ANK repeat; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Long QT syndrome; Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; Repeat; Synapse. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3957 AA 
Protein Sequence
MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY LKGGIDINTC 60
NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA LHIASLAGQA EVVKVLVKEG 120
ANINAQSQNG FTPLYMAAQE NHIDVVKYLL ENGANQSTAT EDGFTPLAVA LQQGHNQAVA 180
ILLENDTKGK VRLPALHIAA RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA 240
AHYGNVNVAT LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL 300
TPLHCAARSG HDQVVELLLE RGAPLLARTK NGLSPLHMAA QGDHVECVKH LLQHKAPVDD 360
VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT PLHIACKKNR IKVMELLVKY 420
GASIQAITES GLTPIHVAAF MGHLNIVLLL LQNGASPDVT NIRGETALHM AARAGQVEVV 480
RCLLRNGALV DARAREEQTP LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE 540
GQVDVASVLL EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL 600
HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN YGAETNIVTK 660
QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH LAAQEDKVNV ADILTKHGAD 720
QDAHTKLGYT PLIVACHYGN VKMVNFLLKQ GANVNAKTKN GYTPLHQAAQ QGHTHIINVL 780
LQHGAKPNAT TANGNTALAI AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT 840
EVLDVSDEEG DDTMTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR 900
SFSSDRSHTL SHASYLRDSA VMDDSVVIPS HQVSTLAKEA ERNSYRLSWG TENLDNVALS 960
SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA PTRVTCRLVK RHRLATMPPM 1020
VEGEGLASRL IEVGPSGAQF LGKLHLPTAP PPLNEGESLV SRILQLGPPG TKFLGPVIVE 1080
IPHFAALRGK ERELVVLRSE NGDSWKEHFC DYTEDELNEI LNGMDEVLDS PEDLEKKRIC 1140
RIITRDFPQY FAVVSRIKQD SNLIGPEGGV LSSTVVPQVQ AVFPEGALTK RIRVGLQAQP 1200
MHSELVKKIL GNKATFSPIV TLEPRRRKFH KPITMTIPVP KASSDVMLNG FGGDAPTLRL 1260
LCSITGGTTP AQWEDITGTT PLTFVNECVS FTTNVSARFW LIDCRQIQES VTFASQVYRE 1320
IICVPYMAKF VVFAKSHDPI EARLRCFCMT DDKVDKTLEQ QENFAEVARS RDVEVLEGKP 1380
IYVDCFGNLV PLTKSGQHHI FSFFAFKENR LPLFVKVRDT TQEPCGRLSF MKEPKSTRGL 1440
VHQAICNLNI TLPIYTKESE SDQEQEEEID MTSEKNDETE STETSVLKSH LVNEVPVLAS 1500
PDLLSEVSEM KQDLIKMTAI LTTDVSDKAG SIKVKELVKA AEEEPGEPFE IVERVKEDLE 1560
KVNEILRSGT CTRDESSVQS SRSERGLVEE EWVIVSDEEI EEARQKAPLE ITEYPCVEVR 1620
IDKEIKGKVE KDSTGLVNYL TDDLNTCVPL PKEQLQTVQD KAGKKCEALA VGRSSEKEGK 1680
DIPPDETQST QKQHKPSLGI KKPVRRKLKE KQKQKEEGLQ ASAEKAELKK GSSEESLGED 1740
PGLAPEPLPT VKATSPLIEE TPIGSIKDKV KALQKRVEDE QKGRSKLPIR VKGKEDVPKK 1800
TTHRPHPAAS PSLKSERHAP GSPSPKTERH STLSSSAKTE RHPPVSPSSK TEKHSPVSPS 1860
AKTERHSPAS SSSKTEKHSP VSPSTKTERH SPVSSTKTER HPPVSPSGKT DKRPPVSPSG 1920
RTEKHPPVSP GRTEKRLPVS PSGRTDKHQP VSTAGKTEKH LPVSPSGKTE KQPPVSPTSK 1980
TERIEETMSV RELMKAFQSG QDPSKHKTGL FEHKSAKQKQ PQEKGKVRVE KEKGPILTQR 2040
EAQKTENQTI KRGQRLPVTG TAESKRGVRV SSIGVKKEDA AGGKEKVLSH KIPEPVQSVP 2100
EEESHRESEV PKEKMADEQG DMDLQISPDR KTSTDFSEVI KQELEDNDKY QQFRLSEETE 2160
KAQLHLDQVL TSPFNTTFPL DYMKDEFLPA LSLQSGALDG SSESLKNEGV AGSPCGSLME 2220
GTPQISSEES YKHEGLAETP ETSPESLSFS PKKSEEQTGE TKESTKTETT TEIRSEKEHP 2280
TTKDITGGSE ERGATVTEDS ETSTESFQKE ATLGSPKDTS PKRQDDCTGS CSVALAKETP 2340
TGLTEEAACD EGQRTFGSSA HKTQTDSEVQ ESTATSDETK ALPLPEASVK TDTGTESKPQ 2400
GVIRSPQGLE LALPSRDSEV LSAVADDSLA VSHKDSLEAS PVLEDNSSHK TPDSLEPSPL 2460
KESPCRDSLE SSPVEPKMKA GIFPSHFPLP AAVAKTELLT EVASVRSRLL RDPDGSAEDD 2520
SLEQTSLMES SGKSPLSPDT PSSEEVSYEV TPKTTDVSTP KPAVIHECAE EDDSENGEKK 2580
RFTPEEEMFK MVTKIKMFDE LEQEAKQKRD YKKEPKQEES SSSSDPDADC SVDVDEPKHT 2640
GSGEDESGVP VLVTSESRKV SSSSESEPEL AQLKKGADSG LLPEPVIRVQ PPSPLPSSMD 2700
SNSSPEEVQF QPVVSKQYTF KMNEDTQEEP GKSEEEKDSE SHLAEDRHAV STEAEDRSYD 2760
KLNRDTDQPK ICDGHGCEAM SPSSSAAPVS SGLQSPTGDD VDEQPVIYKE SLALQGTHEK 2820
DTEGEELDVS RAESPQADCP SESFSSSSSL PHCLVSEGKE LDEDISATSS IQKTEVTKTD 2880
ETFENLPKDC PSQDSSITTQ TDRFSMDVPV SDLAENDEIY DPQITSPYEN VPSQSFFSSE 2940
ESKTQTDANH TTSFHSSEVY SVTITSPVED VVVASSSSGT VLSKESNFEG QDIKMESQQE 3000
STLWEMQSDS VSSSFEPTMS ATTTVVGEQI SKVIITKTDV DSDSWSEIRE DDEAFEARVK 3060
EEEQKIFGLM VDRQSQGTTP DTTPARTPTE EGTPTSEQNP FLFQEGKLFE MTRSGAIDMT 3120
KRSYADESFH FFQIGQESRE ETLSEDVKEG ATGADPLPLE TSAESLALSE SKETVDDEAD 3180
LLPDDVSEEV EEIPASDAQL NSQMGISAST ETPTKEAVSV GTKDLPTVQT GDIPPLSGVK 3240
QISCPDSSEP AVQVQLDFST LTRSVYSDRG DDSPDSSPEE QKSVIEIPTA PMENVPFTES 3300
KSKIPVRTMP TSTPAPPSAE YESSVSEDFL SSVDEENKAD EAKPKSKLPV KVPLQRVEQQ 3360
LSDLDTSVQK TVAPQGQDMA SIAPDNRSKS ESDASSLDSK TKCPVKTRSY TETETESRER 3420
AEELELESEE GATRPKILTS RLPVKSRSTT SSCRGGTSPT KESKEHFFDL YRNSIEFFEE 3480
ISDEASKLVD RLTQSEREQE IVSDDESSSA LEVSVIENLP PVETEHSVPE DIFDTRPIWD 3540
ESIETLIERI PDENGHDHAE DPQDEQERIE ERLAYIADHL GFSWTELARE LDFTEEQIHQ 3600
IRIENPNSLQ DQSHALLKYW LERDGKHATD TNLVECLTKI NRMDIVHLME TNTEPLQERI 3660
SHSYAEIEQT ITLDHSEGFS VLQEELCTAQ HKQKEEQAVS KESETCDHPP IVSEEDISVG 3720
YSTFQDGVPK TEGDSSATAL FPQTHKEQVQ QDFSGKMQDL PEESSLEYQQ EYFVTTPGTE 3780
TSETQKAMIV PSSPSKTPEE VSTPAEEEKL YLQTPTSSER GGSPIIQEPE EPSEHREESS 3840
PRKTSLVIVE SADNQPETCE RLDEDAAFEK GDDMPEIPPE TVTEEEYIDE HGHTVVKKVT 3900
RKIIRRYVSS EGTEKEEIMV QGMPQEPVNI EEGDGYSKVI KRVVLKSDTE QSEDNNE 3957 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
 GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
 GO:0043034; C:costamere; ISS:BHF-UCL.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005887; C:integral to plasma membrane; IEA:Compara.
 GO:0014704; C:intercalated disc; ISS:BHF-UCL.
 GO:0031430; C:M band; ISS:BHF-UCL.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0030315; C:T-tubule; ISS:BHF-UCL.
 GO:0030018; C:Z disc; ISS:BHF-UCL.
 GO:0051117; F:ATPase binding; ISS:BHF-UCL.
 GO:0044325; F:ion channel binding; ISS:BHF-UCL.
 GO:0015459; F:potassium channel regulator activity; IEA:Compara.
 GO:0030674; F:protein binding, bridging; ISS:BHF-UCL.
 GO:0003283; P:atrial septum development; IMP:BHF-UCL.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0060048; P:cardiac muscle contraction; IEA:Compara.
 GO:0006874; P:cellular calcium ion homeostasis; ISS:BHF-UCL.
 GO:0086046; P:membrane depolarization involved in regulation of SA node cell action potential; TAS:BHF-UCL.
 GO:1901021; P:positive regulation of calcium ion transmembrane transporter activity; ISS:BHF-UCL.
 GO:0051928; P:positive regulation of calcium ion transport; ISS:BHF-UCL.
 GO:2001259; P:positive regulation of cation channel activity; ISS:BHF-UCL.
 GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
 GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISS:BHF-UCL.
 GO:0043268; P:positive regulation of potassium ion transport; ISS:BHF-UCL.
 GO:0034394; P:protein localization to cell surface; ISS:BHF-UCL.
 GO:0070972; P:protein localization to endoplasmic reticulum; IGI:BHF-UCL.
 GO:0036309; P:protein localization to M-band; ISS:BHF-UCL.
 GO:0036371; P:protein localization to T-tubule; ISS:BHF-UCL.
 GO:0050821; P:protein stabilization; ISS:BHF-UCL.
 GO:0072661; P:protein targeting to plasma membrane; IEA:Compara.
 GO:0086014; P:regulation of atrial cardiac muscle cell action potential; IMP:BHF-UCL.
 GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IGI:BHF-UCL.
 GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
 GO:0086005; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
 GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
 GO:0070296; P:sarcoplasmic reticulum calcium ion transport; TAS:BHF-UCL.
 GO:0033292; P:T-tubule organization; ISS:BHF-UCL. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR011029; DEATH-like_dom.
 IPR000488; Death_domain.
 IPR000906; ZU5. 
Pfam
 PF00023; Ank
 PF12796; Ank_2
 PF00531; Death
 PF00791; ZU5 
SMART
 SM00248; ANK
 SM00005; DEATH 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS50017; DEATH_DOMAIN
 PS51145; ZU5 
PRINTS
 PR01415; ANKYRIN.