CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018355
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nesprin-2 
Protein Synonyms/Alias
 Nuclear envelope spectrin repeat protein 2; Nucleus and actin connecting element protein; Protein NUANCE; Synaptic nuclear envelope protein 2; Syne-2 
Gene Name
 SYNE2 
Gene Synonyms/Alias
 KIAA1011; NUA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
955KLSDNILKLEKQINKacetylation[1]
1758REDLDQAKTQIGMTEacetylation[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] 
Functional Description
 Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. Component of SUN-protein- containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Involved in the maintenance of nuclear organization and structural integrity. Connects nuclei to the cytoskeleton by interacting with the nuclear envelope and with F-actin in the cytoplasm. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for centrosome migration to the apical cell surface during early ciliogenesis. 
Sequence Annotation
 DOMAIN 1 286 Actin-binding.
 DOMAIN 31 136 CH 1.
 DOMAIN 181 286 CH 2.
 REPEAT 4944 5053 Spectrin 1.
 REPEAT 5054 5167 Spectrin 2.
 REPEAT 5170 5274 Spectrin 3.
 REPEAT 5852 5914 Spectrin 4.
 REPEAT 5917 6019 Spectrin 5.
 REPEAT 6022 6133 Spectrin 6.
 REPEAT 6136 6242 Spectrin 7.
 REPEAT 6245 6349 Spectrin 8.
 REPEAT 6551 6658 Spectrin 9.
 DOMAIN 6826 6885 KASH.
 MOD_RES 955 955 N6-acetyllysine.
 MOD_RES 2781 2781 Phosphoserine.
 MOD_RES 4108 4108 Phosphoserine.
 MOD_RES 6361 6361 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Actin-binding; Alternative splicing; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Emery-Dreifuss muscular dystrophy; Membrane; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Sarcoplasmic reticulum; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 6885 AA 
Protein Sequence
MASSPELPTE DEQGSWGIDD LHISLQAEQE DTQKKAFTCW INSQLARHTS PSVISDLFTD 60
IKKGHVLLDL LEVLSGQQLP RDKGSNTFQC RINIEHALTF LRNRSIKLIN IHVTDIIDGN 120
PSIILGLIWT IILHFHIEKL AQTLSCNYNQ PSLDDVSVVD SSPASSPPAK KCSKVQARWQ 180
MSARKALLLW AQEQCATYES VNVTDFKSSW RNGMAFLAII HALRPDLIDM KSVKHRSNKD 240
NLREAFRIAE QELKIPRLLE PEDVDVVDPD EKSIMTYVAQ FLQYSKDAPG TGEEAQGKVK 300
DAMGWLTLQK EKLQKLLKDS ENDTYFKKYN SLLSFMESFN EEKKSFLDVL SIKRDLDELD 360
KDHLQLREAW DGLDHQINAW KIKLNYALPP PLHQTEAWLQ EVEELMDEDL SASQDHSQAV 420
TLIQEKMTLF KSLMDRFEHH SNILLTFENK DENHLPLVPP NKLEEMKRRI NNILEKKFIL 480
LLEFHYYKCL VLGLVDEVKS KLDIWNIKYG SRESVELLLE DWHKFIEEKE FLARLDTSFQ 540
KCGEIYKNLA GECQNINKQY MMVKSDVCMY RKNIYNVKST LQKVLACWAT YVENLRLLRA 600
CFEETKKEEI KEVPFETLAQ WNLEHATLNE AGNFLVEVSN DVVGSSISKE LRRLNKRWRK 660
LVSKTQLEMN LPLMIKKQDQ PTFDNSGNIL SKEEKATVEF STDMSVELPE NYNQNIKAGE 720
KHEKENEEFT GQLKVAKDVE KLIGQVEIWE AEAKSVLDQD DVDTSMEESL KHLIAKGSMF 780
DELMARSEDM LQMDIQNISS QESFQHVLTT GLQAKIQEAK EKVQINVVKL IAALKNLTDV 840
SPDLDIRLKM EESQKELESY MMRAQQLLGQ RESPGELISK HKEALIISNT KSLAKYLKAV 900
EELKNNVTED IKMSLEEKSR DVCAKWESLH HELSLYVQQL KIDIEKGKLS DNILKLEKQI 960
NKEKKLIRRG RTKGLIKEHE ACFSEEGCLY QLNHHMEVLR ELCEELPSQK SQQEVKRLLK 1020
DYEQKIERLL KCASEIHMTL QPTAGGTSKN EGTITTSENR GGDPHSEAPF AKSDNQPSTE 1080
KAMEPTMKFS LASVLRPLQE ESIMEKDYSA SINSLLERYD TYRDILEHHL QNNKFRITSD 1140
FSSEEDRSSS CLQAKLTDLQ VIKNETDARW KEFEIISLKL ENHVNDIKKP FVIKERDTLK 1200
ERERELQMTL NTRMESLETA LRLVLPVEKA SLLLCGSDLP LHKMAIQGFH LIDADRIYQH 1260
LRNIQDSIAK QIEICNRLEE PGNFVLKELH PFDLHAMQNI ILKYKTQFEG MNHRVQRSED 1320
TLKALEDFLA SLRTAKLSAE PVTDLSASDT QVAQENTLTV KNKEGEIHLM KDKAKHLDKC 1380
LKMLDMSFKD AERGDDTSCE NLLDAFSIKL SETHGYGVQE EFTEENKLLE ACIFKNNELL 1440
KNIQDVQSQI SKIGLKDPTV PAVKHRKKSL IRLDKVLDEY EEEKRHLQEM ANSLPHFKDG 1500
REKTVNQQCQ NTVVLWENTK ALVTECLEQC GRVLELLKQY QNFKSILTTL IQKEESVISL 1560
QASYMGKENL KKRIAEIEIV KEEFNEHLEV VDKINQVCKN LQFYLNKMKT FEEPPFEKEA 1620
NIIVDRWLDI NEKTEDYYEN LGRALALWDK LFNLKNVIDE WTEKALQKME LHQLTEEDRE 1680
RLKEELQVHE QKTSEFSRRV AEIQFLLQSS EIPLELQVME SSILNKMEHV QKCLTGESNC 1740
HALSGSTAEL REDLDQAKTQ IGMTESLLKA LSPSDSLEIF TKLEEIQQQI LQQKHSMILL 1800
ENQIGCLTPE LSELKKQYES VSDLFNTKKS VLQDHFSKLL NDQCKNFNDW FSNIKVNLKE 1860
CFESSETKKS VEQKLQKLSD FLTLEGRNSK IKQVDSVLKH VKKHLPKAHV KELISWLVGQ 1920
EFELEKMESI CQARAKELED SLQQLLRLQD DHRNLRKWLT NQEEKWKGME EPGEKTELFC 1980
QALARKREQF ESVAQLNNSL KEYGFTEEEE IIMEATCLMD RYQTLLRQLS EIEEEDKLLP 2040
TEDQSFNDLA HDVIHWIKEI KESLMVLNSS EGKMPLEERI QKIKEIILLK PEGDARIETI 2100
MKQAESSEAP LVQKTLTDIS NQWDNTLHLA STYLSHQEKL LLEGEKYLQS KEDLRLMLIE 2160
LKKKQEAGFA LQHGLQEKKA QLKIYKKFLK KAQDLTSLLK ELKSQGNYLL ECTKNPSFSE 2220
EPWLEIKHLH ESLLQQLQDS VQNLDGHVRE HDSYQVCVTD LNTTLDNFSK EFVSFSDKPV 2280
DQIAVEEKLQ KLQELENRLS LQDGTLKKIL ALAKSVKQNT SSVGQKIIKD DIKSLQCKQK 2340
DLENRLASAK QEMECCLNSI LKSKRSTEKK GKFTLPGREK QATSDVQEST QESAAVEKLE 2400
EDWEINKDSA VEMAMSKQLS LNAQESMKNT EDERKVNELQ NQPLELDTML RNEQLEEIEK 2460
LYTQLEAKKA AIKPLEQTEC LNKTETGALV LHNIGYSAQH LDNLLQALIT LKKNKESQYC 2520
VLRDFQEYLA AVESSMKALL TDKESLKVGP LDSVTYLDKI KKFIASIEKE KDSLGNLKIK 2580
WENLSNHVTD MDKKLLESQI KQLEHGWEQV EQQIQKKYSQ QVVEYDEFTT LMNKVQDTEI 2640
SLQQQQQHLQ LRLKSPEERA GNQSMIALTT DLQATKHGFS VLKGQAELQM KRIWGEKEKK 2700
NLEDGINNLK KQWETLEPLH LEAENQIKKC DIRNKMKETI LWAKNLLGEL NPSIPLLPDD 2760
ILSQIRKCKV THDGILARQQ SVESLAEEVK DKVPSLTTYE GSDLNNTLED LRNQYQMLVL 2820
KSTQRSQQLE FKLEERSNFF AIIRKFQLMV QESETLIIPR VETAATEAEL KHHHVTLEAS 2880
QKELQEIDSG ISTHLQELTN IYEELNVFER LFLEDQLKNL KIRTNRIQRF IQNTCNEVEH 2940
KIKFCRQFHE KTSALQEEAD SIQRNELLLN QEVNKGVKEE IYNLKDRLTA IKCCILQVLK 3000
LKKVFDYIGL NWDFSQLDQL QTQVFEKEKE LEEKIKQLDT FEEEHGKYQA LLSKMRAIDL 3060
QIKKMTEVVL KAPDSSPESR RLNAQILSQR IEKAKCLCDE IIKKLNENKT FDDSFKEKEI 3120
LQIKLNAEEN DKLYKVLQNM VLELSPKELD EKNCQDKLET SLHVLNQIKS QLQQPLLINL 3180
EIKHIQNEKD NCEAFQEQVW AEMCSIKAVT AIEKQREENS SEASDVETKL REFEDLQMQL 3240
NTSIDLRTNV LNDAYENLTR YKEAVTRAVE SITSLEAIII PYRVDVGNPE ESLEMPLRKQ 3300
EELESTVAHI QDLTEKLGMI SSPEAKLQLQ YTLQELVSKN SAMKEAFKAQ ETEAERYLEN 3360
YKCYRKMEED IYTNLSKMET VLGQSMSSLP LSYREALERL EQSKALVSNL ISTKEELMKL 3420
RQILRLLRLR CTENDGICLL KIVSALWEKW LSLLEAAKEW EMWCEELKQE WKFVSEEIER 3480
EAIILDNLQE ELPEISKTKE AATTEELSEL LDCLCQYGEN VEKQQLLLTL LLQRIRSIQN 3540
VPESSGAVET VPAFQEITSM KERCNKLLQK VQKNKELVQT EIQERHSFTK EIIALKNFFQ 3600
QTTTSFQNMA FQDHPEKSEQ FEELQSILKK GKLTFENIME KLRIKYSEMY TIVPAEIESQ 3660
VEECRKALED IDEKISNEVL KSSPSYAMRR KIEEINNGLH NVEKMLQQKS KNIEKAQEIQ 3720
KKMWDELDLW HSKLNELDSE VQDIVEQDPG QAQEWMDNLM IPFQQYQQVS QRAECRTSQL 3780
NKATVKMEEY SDLLKSTEAW IENTSHLLAN PADYDSLRTL SHHASTVQMA LEDSEQKHNL 3840
LHSIFMDLED LSIIFETDEL TQSIQELSNQ VTALQQKIME SLPQIQRMAD DVVAIESEVK 3900
SMEKRVSKIK TILLSKEIFD FSPEEHLKHG EVILENIRPM KKTIAEIVSY QVELRLPQTG 3960
MKPLPVFQRT NQLLQDIKLL ENVTQEQNEL LKVVIKQTNE WDEEIENLKQ ILNNYSAQFS 4020
LEHMSPDQAD KLPQLQGEIE RMEKQILSLN QRKEDLLVDL KATVLNLHQH LKQEQEGVER 4080
DRLPAVTSEE GGVAERDASE RKLNRRGSMS YLAAVEEEVE ESSVKSDNGD EKAEPSPQSW 4140
SSLWKHDKDM EEDRASSSSG TIVQEAYGKI STSDNSMAQI LTPDSLNTEQ GPECSLRPNQ 4200
TEEGTTPPIE ADTLDSSDAQ GGLEPRVEKT RPEPTEVLHA CKTQVAELEL WLQQANVAVE 4260
PETLNADMQQ VLEQQLVGCQ AMLTEIEHKV AFLLETCKDQ GLGDNGATQH EAEALSLKLK 4320
TVKCNLEKVQ MMLQEKHSED QHPTILKKSS EPEHQEALQP VNLSELESIV TERPQFSRQK 4380
DFQQQQVLEL KPMEQKDFIK FIEFNAKKMW PQYCQHDNDT TQESSASNQA SSPENDVPDS 4440
ILSPQGQNGD KWQYLHHELS SKIKLPLPQL VEPQVSTNMG ILPSVTMYNF RYPTTEELKT 4500
YTTQLEDLRQ EASNLQTQEN MTEEAYINLD KKLFELFLTL SQCLSSVEEM LEMPRLYRED 4560
GSGQQVHYET LALELKKLYL ALSDKKGDLL KAMTWPGENT NLLLECFDNL QVCLEHTQAA 4620
AVCRSKSLKA GLDYNRSYQN EIKRLYHQLI KSKTSLQQSL NEISGQSVAE QLQKADAYTV 4680
ELENAESRVA KLRDEGERLH LPYALLQEVY KLEDVLDSMW GMLRARYTEL SSPFVTESQQ 4740
DALLQGMVEL VKIGKEKLAH GHLKQTKSKV ALQAQIENHK VFFQKLVADM LLIQAYSAKI 4800
LPSLLQNRET FWAEQVTEVK ILEEKSRQCG MKLQSLLQKW EEFDENYASL EKDLEILIST 4860
LPSVSLVEET EERLVERISF YQQIKRNIGG KHARLYQTLN EGKQLVASVS CPELEGQIAK 4920
LEEQWLSLNK KIDHELHRLQ ALLKHLLSYN RDSDQLTKWL ESSQHTLNYW KEQSLNVSQD 4980
LDTIRSNINN FFEFSKEVDE KSSLKTAVIS IGNQLLHLKE TDTATLRASL AQFEQKWTML 5040
ITQLPDIQEK LHQLQMEKLP SRKAITEMIS WMNNVEHQTS DEDSVHSPSS ASQVKHLLQK 5100
HKEFRMEMDY KQWIVDFVNQ SLLQLSTCDV ESKRYERTEF AEHLGEMNRQ WHRVHGMLNR 5160
KIQHLEQLLE SITESENKIQ ILNNWLEAQE ERLKTLQKPE SVISVQKLLL DCQDIENQLA 5220
IKSKALDELK QSYLTLESGA VPLLEDTASR IDELFQKRSS VLTQVNQLKT SMQSVLQEWK 5280
IYDQLYDEVN MMTIRFWYCM EHSKPVVLSL ETLRCQVENL QSLQDEAESS EGSWEKLQEV 5340
IGKLKGLCPS VAEIIEEKCQ NTHKRWTQVN QAIADQLQKA QSLLQLWKAY SNAHGEAAAR 5400
LKQQEAKFQQ LANISMSGNN LAEILPPALQ DIKELQHDVQ KTKEAFLQNS SVLDRLPQPA 5460
ESSTHMLLPG PLHSLQRAAY LEKMLLVKAN EFEFVLSQFK DFGVRLESLK GLIMHEEENL 5520
DRLHQQEKEN PDSFLNHVLA LTAQSPDIEH LNEVSLKLPL SDVAVKTLQN MNRQWIRATA 5580
TALERCSELQ GIGLNEKFLY CCEKWIQLLE KIEEALKVDV ANSLPELLEQ QKTYKMLEAE 5640
VSINQTIADS YVTQSLQLLD TTEIENRPEF ITEFSKLTDR WQNAVQGVRQ RKGDVDGLVR 5700
QWQDFTTSVE NLFRFLTDTS HLLSAVKGQE RFSLYQTRSL IHELKNKEIH FQRRRTTCAL 5760
TLEAGEKLLL TTDLKTKESV GRRISQLQDS WKDMEPQLAE MIKQFQSTVE TWDQCEKKIK 5820
ELKSRLQVLK AQSEDPLPEL HEDLHNEKEL IKELEQSLAS WTQNLKELQT MKADLTRHVL 5880
VEDVMVLKEQ IEHLHRQWED LCLRVAIRKQ EIEDRLNTWV VFNEKNKELC AWLVQMENKV 5940
LQTADISIEE MIEKLQKDCM EEINLFSENK LQLKQMGDQL IKASNKSRAA EIDDKLNKIN 6000
DRWQHLFDVI GSRVKKLKET FAFIQQLDKN MSNLRTWLAR IESELSKPVV YDVCDDQEIQ 6060
KRLAEQQDLQ RDIEQHSAGV ESVFNICDVL LHDSDACANE TECDSIQQTT RSLDRRWRNI 6120
CAMSMERRMK IEETWRLWQK FLDDYSRFED WLKSAERTAA CPNSSEVLYT SAKEELKRFE 6180
AFQRQIHERL TQLELINKQY RRLARENRTD TASRLKQMVH EGNQRWDNLQ RRVTAVLRRL 6240
RHFTNQREEF EGTRESILVW LTEMDLQLTN VEHFSESDAD DKMRQLNGFQ QEITLNTNKI 6300
DQLIVFGEQL IQKSEPLDAV LIEDELEELH RYCQEVFGRV SRFHRRLTSC TPGLEDEKEA 6360
SENETDMEDP REIQTDSWRK RGESEEPSSP QSLCHLVAPG HERSGCETPV SVDSIPLEWD 6420
HTGDVGGSSS HEEDEEGPYY SALSGKSISD GHSWHVPDSP SCPEHHYKQM EGDRNVPPVP 6480
PASSTPYKPP YGKLLLPPGT DGGKEGPRVL NGNPQQEDGG LAGITEQQSG AFDRWEMIQA 6540
QELHNKLKIK QNLQQLNSDI SAITTWLKKT EAELEMLKMA KPPSDIQEIE LRVKRLQEIL 6600
KAFDTYKALV VSVNVSSKEF LQTESPESTE LQSRLRQLSL LWEAAQGAVD SWRGGLRQSL 6660
MQCQDFHQLS QNLLLWLASA KNRRQKAHVT DPKADPRALL ECRRELMQLE KELVERQPQV 6720
DMLQEISNSL LIKGHGEDCI EAEEKVHVIE KKLKQLREQV SQDLMALQGT QNPASPLPSF 6780
DEVDSGDQPP ATSVPAPRAK QFRAVRTTEG EEETESRVPG STRPQRSFLS RVVRAALPLQ 6840
LLLLLLLLLA CLLPSSEEDY SCTQANNFAR SFYPMLRYTN GPPPT 6885 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0031527; C:filopodium membrane; IDA:UniProtKB.
 GO:0005925; C:focal adhesion; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
 GO:0044429; C:mitochondrial part; IDA:UniProtKB.
 GO:0031981; C:nuclear lumen; IDA:UniProtKB.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
 GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0034993; C:SUN-KASH complex; IDA:UniProtKB.
 GO:0030018; C:Z disc; IDA:UniProtKB.
 GO:0003779; F:actin binding; ISS:UniProtKB.
 GO:0051642; P:centrosome localization; IMP:UniProtKB.
 GO:0090286; P:cytoskeletal anchoring at nuclear membrane; IDA:UniProtKB.
 GO:0007163; P:establishment or maintenance of cell polarity; IEA:Compara.
 GO:0010761; P:fibroblast migration; IEA:Compara.
 GO:0006998; P:nuclear envelope organization; IEA:Compara.
 GO:0031022; P:nuclear migration along microfilament; ISS:UniProtKB.
 GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
 GO:0034504; P:protein localization to nucleus; IEA:Compara. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR012315; KASH.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF10541; KASH
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS51049; KASH 
PRINTS