CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018612
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dystonin 
Protein Synonyms/Alias
 Bullous pemphigoid antigen 1; BPA; Dystonia musculorum protein; Hemidesmosomal plaque protein; Microtubule actin cross-linking factor 2 
Gene Name
 Dst 
Gene Synonyms/Alias
 Bpag1; Macf2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
5731SMKKKLDKVLKKYDAacetylation[1]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 
Functional Description
 Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin- containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two- dimensional mesh. May regulate the organization and stability of the microtubule network of sensory neurons to allow axonal transport. 
Sequence Annotation
 DOMAIN 35 252 Actin-binding.
 DOMAIN 35 138 CH 1.
 DOMAIN 151 252 CH 2.
 REPEAT 701 801 Spectrin 1.
 DOMAIN 889 941 SH3.
 REPEAT 1582 1624 Plectin 1.
 REPEAT 1657 1701 Plectin 2.
 REPEAT 1772 1815 Plectin 3.
 REPEAT 1816 1844 Plectin 4.
 REPEAT 1848 1889 Plectin 5.
 REPEAT 3845 3925 Spectrin 2.
 REPEAT 3997 4079 Spectrin 3.
 REPEAT 4440 4548 Spectrin 4.
 REPEAT 4552 4657 Spectrin 5.
 REPEAT 4775 4877 Spectrin 6.
 REPEAT 5208 5315 Spectrin 7.
 REPEAT 5322 5423 Spectrin 8.
 REPEAT 5430 5532 Spectrin 9.
 REPEAT 5647 5751 Spectrin 10.
 REPEAT 5758 5856 Spectrin 11.
 REPEAT 6002 6082 Spectrin 12.
 REPEAT 6089 6191 Spectrin 13.
 REPEAT 6197 6300 Spectrin 14.
 REPEAT 6308 6410 Spectrin 15.
 REPEAT 6415 6519 Spectrin 16.
 REPEAT 6523 6629 Spectrin 17.
 REPEAT 6636 6736 Spectrin 18.
 REPEAT 6741 6844 Spectrin 19.
 DOMAIN 7015 7050 EF-hand 1.
 DOMAIN 7051 7086 EF-hand 2.
 DOMAIN 7091 7169 GAR.
 MOTIF 1382 1388 Nuclear localization signal; in isoform
 MOTIF 7369 7372 Microtubule tip localization signal.
 MOD_RES 2857 2857 Phosphoserine (By similarity).
 MOD_RES 7182 7182 Phosphoserine.
 MOD_RES 7250 7250 Phosphoserine (By similarity).  
Keyword
 3D-structure; Actin-binding; Alternative promoter usage; Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Endoplasmic reticulum; Intermediate filament; Lipoprotein; Membrane; Metal-binding; Microtubule; Muscle protein; Myristate; Nucleus; Palmitate; Phosphoprotein; Reference proteome; Repeat; SH3 domain; Transmembrane. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 7389 AA 
Protein Sequence
MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY 60
EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD 120
GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG VRCENFTTCW 180
RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE 240
KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP 300
NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK 360
EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC EDKLILARNA LQSDSKRLES 420
GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC 480
SSVYSKGRML TTEQTKLMIS GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS 540
SGMTSRLTPS VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 600
EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI 660
SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT LHNFVTRATN ELIWLNEKEE 720
SEVAYDWSER NSSVARKKSY HVELMRELEQ KEESIKAVQE IAEQLLLENH PARLTIEAYR 780
AAMQTQWSWI LQLCQCVEQH IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI 840
HKLEDLVQES MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI 900
EITIYKDDEC VLANNSHRAK WKVISPTGNE AVVPSVCFTV PPPNKEAVDF ANRIEQQYQS 960
VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML PGEHQQVLSN LQSRLEDFLE 1020
DSQESQIFSG SDISQLEKEV SVCRKYYQEL LKSAEREEQE ESVYNLYISE VRNIRLRLES 1080
CEDRLIRQIR TPLERDDLHE SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP 1140
SVPALRSELS VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV 1200
IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK ERDLDFDWHK 1260
EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP LDDWIQHIET TQRKIQENQP 1320
ENSKALALQL NQQKMLVSEI EVKQSKMDEC QKYSEQYSAA VKDYELQTMT YRAMVESQQK 1380
SPVKRRRIQS SADLVIQEFM DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ 1440
HIEKAKELQK WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK 1500
HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD KVIAGTINQT 1560
TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR KCFDLRDAES HGLIDEQVLR 1620
QLKELNRAKQ LISTASPTSI PVLDSLAQGM VSESMAIRVL EILLSAGPLL VPATGEHLTL 1680
QQAFQQNLIS SALFSKVLER QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP 1740
QEAGRITLKC GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE 1800
GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL EAQRGYVGLI 1860
WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP ESSQVIGLDA AKQLGIIDNN 1920
TASVLKDVKL PDKMPDLGDL EDCKNAKRWL SFCKFQPSTV HDYRQEEGGS DGEEPVTAQS 1980
SEQTKKLFLS YLMVNSYMDA HTGQRLLLYD GDLDEAVSML LESCGAELGA DTSTRESLSV 2040
LTIPDAFPDC ALSEEKHECS ADKCHYSHPG HKESLENAKW DMNEAFCKMG NNDSNGELPR 2100
PENLADTTVV QKGSESPSRV RVPKPTSSST QPEGSVLRPE SGSILKGCKS QSEPVTKKYP 2160
DGTNHSHFLT SETSRPCDSN EREDEENIQK GPSVFDYSPR LSALLSHDEL RQSQGRFSDT 2220
STPQNTGYLC EASTLSPSDQ RVLADQSTRE KFQDRFLGIA AISVSLQGAP CGQKPVDTEC 2280
SSSQVHYHSE ESMSDASAES GATRQTDESE KTGSKVEDNS CTMVPGGGSR NDNTSDCGPL 2340
SHKGAIDAGD YETSLLAGQQ SDTATDSDSD DYFYDTPLFE DEDHDSLILQ GDDRDCLQPE 2400
DYDTSLQEEN DRTPPPDDIF YDVMKEKENP EFPHGGMDES LGVENKVCCP QGFPVGIEKP 2460
ELYLAGEKEF NSGGSEQLVE SVSESENPPG LWDSESDSLT EGEIIGRKER LGASLTPDGH 2520
WRGDREECDT SRESQSDTDG VGSIQSSESY RPYMSDGSDL DEEDNGGRSS EDSGDGRGGQ 2580
GVADEGGEPQ YQADPTQLYT AIRKEHGGET QNVSDMIPLD KTHSYSPLET QHGAGVFQPE 2640
SAGKGGWDTE RSSHPELTTE ADEEDEASLS THMATKGVSL SNAEGTASEE IRLVQGPDSS 2700
GILKAEDLEN VSPEISPSSD NIVRSEAELG GGASEDGHLS FTGSDRDQQG PGRGLVKGRD 2760
GQSDKLVDET SIREMGFQKE GVLMSSPEEG GEEERDLEPF PNGSATESLN MGKSQVPPLL 2820
THTEELSHRG APHTTTMTTT MTLEGEAKNV QTGLTESPVL LETLAEIFDT PASKVTRADL 2880
TSAVTASEMK SQVKEDSLTG GPEKETGPCT SLGHCDKCIH VDMLEPNEHT PSCALVAPPT 2940
VKDNLCSVNN AGEKSVRPQE DWPPAAEVRL SDACVEESIS EGKAGILQFT PENSDSTLSR 3000
LPHQSVAGWG KSADSVQARL PVSGVRHTSA DTLDVGCPQL ESSREKASAE EEPHRERALS 3060
LKPQEREHHM LGFVEDGRSI LKSSLDKVHM NLQEVGDPSA GTGTKISIQN LIRRAILSEL 3120
PNEVSNVPSH GISPISNSSE VRAESGGDPF CITSFLHLLK QNQPPQETPG ISELAKVLTQ 3180
MDCDPEQRGL GSELLPPQLK NAFYKLLFDG YATEKDQAEA LGQTSCAVPK MAEEKPHVCS 3240
DLRNKEGHHC PLNPQAVGEA EVEPFSVHIA ALPGGEKLGE LCSEPPEHSE STSGSKERSS 3300
DGSSKEKCSN GLQQCLQHTE KMHEYLVLLQ DMKPPLDNQA SVESSLEALK SQLKQLEAFE 3360
LGLAPIAVFL RKDLKLAEEF LKSFPSDLPR RHHEELSKSH QRLQNAFSSL SSVSSERMKL 3420
IKLAINSEMS KLAVRHEDFL HKLTSYSDWV SEKSRSVKAI QTVNVQDTEL VKNSVKFLKN 3480
VLADLSHTKM QLETTAFDVQ SFISDYAQDL SPSQSRQLLR LLNTTQKGFL DLQELVTTEA 3540
DRLEALLQLE QELGHQKVVA ERQQEYREKL QGLCDLLTQT ENRLISNQEA FVIGDGTVEL 3600
QKYQSKQEEL QRDMQGSTQA MEEIVRNTEL FLKESGDELS QADRALIEQK LNEVKMKCAQ 3660
LNLKAEQSRK ELDKAVTTAL KEETEKVAAV RQLEESKTKI ENLLNWLSNV EEDSEGVWTK 3720
HTQPMEQNGT YLHEGDSKLG AGEEDEVNGN LLETDAEGHS EATKGNLNQQ YEKVKAQHGK 3780
IMAQHQAVLL ATQSAQVLLE KQGHYLSPEE KEKLQKNTQE LKVHYEKVLA ECEKKVKLTH 3840
SLQEELEKFD TDYSEFEHWL QQSEQELANL EAGADDLSGL MDKLTRQKSF SEDVISHKGD 3900
LRYITISGNR VIDAAKSCSK RDSDRIGKDS VETSATHREV QTKLDQVTDR FRSLYSKCSV 3960
LGNNLKDLVD QYQQYEDASC GLLSGLQACE AKASKHLREP IALDPKNLQR QLEETKALQG 4020
QISSQQVAVE KLKKTAEVLL DAKGSLLPAK NDIQKTLDDI VGRYDDLSKC VNERNEKLQI 4080
TLTRSLSVQD ALDEMLDWMG SVESSLVKPG QVPLNSTALQ DLISKDTMLE QDITGRQSSI 4140
NAMNEKVKTF IETTDPSTAS SLQAKMKDLS ARFSEASQKH KEKLAKMVEL KAKVEQFEKL 4200
SDKLQTFLET QSQALTEVAM PGKDVPELSQ HMQESTAKFL EHRKDLEALH SLLKEISSHG 4260
LPGDKALVFE KTNNLSRKFK EMEDTIQEKK DALSSCQEQL SAFQTLAQSL KTWIKETTKQ 4320
VPVVKPSLGT EDLRKSLEET KKLQEKWNLK APEIHKASNS GVSLCNLLSA LISPAKAIAA 4380
AKSGGVILNG EGTDTNTQDF LANKGLTSIK KDMTDISHSY EDLGLLLKDK IVELNTKLSK 4440
LQKAQEESSA MMQWLEKMNK TASRWRQTPT PADTESVKLQ VEQNKSFEAE LKQNVNKVQE 4500
LKDKLSELLE ENPEAPEAQS WKQALAEMDT KWQELNQLTM DRQQKLEESS NNLTQFQTTE 4560
AQLKQWLMEK ELMVSVLGPL SIDPNMLNTQ KQQVQILLQE FDTRKPQYEQ LTAAGQGILS 4620
RPGEDPSLHG IVNEQLEAVT QKWDNLTGQL RDRCDWIDQA IVKSTQYQSL LRSLSGTLTE 4680
LDDKLSSGLT SGALPDAVNQ QLEAAQRLKQ EIEQQAPKIK EAQEVCEDLS ALVKEEYLKA 4740
ELSRQLEGIL KSFKDIEQKT ENHVQHLQSA CASSHQFQQM SKDFQAWLDA KKEEQRDSPP 4800
ISAKLDVLES LLNSQKDFGK TFTEQSNIYE KTISEGENLL LKTQGAEKAA LQLQLNTMKT 4860
DWDRFRKQVK EREEKLKDSL EKALKYREQV ETLRPWIDRC QHSLDGVTFS LDPTESESSI 4920
AELKSLQKEM DHHFGMLELL NNTANSLLSV CEVDKEAVTE ENQSLMEKVN RVTEQLQSKT 4980
VSLENMAQKF KEFQEVSRDT QRQLQDTKEQ LEVHHSLGPQ AYSNKHLSVL QAQQKSLQTL 5040
KQQVDEAKRL AQDLVVEAAD SKGTSDVLLQ AETLAEEHSE LSQQVDEKCS FLETKLQGLG 5100
HFQNTIREMF SQFTECDDEL DGMAPVGRDA ETLRKQKACM QTFLKKLEAL MASNDSANRT 5160
CKMMLATEET SPDLIGVKRD LEALSKQCNK LLDRAKTREE QVDGATEKLE EFHRKLEEFS 5220
TLLQKAEEHE ESQGPVGTET ETINQQLDVF KVFQKEEIEP LQVKQQDVNW LGQGLIQSAA 5280
ANTCTQGLEH DLDSVNSRWK TLNKKVAQRT SQLQEALLHC GRFQDALESL LSWMADTEEL 5340
VANQKPPSAE FKVVKAQIQE QKLLQRLLED RKSTVEVIKR EGEKIAASAE PADRVKLTRQ 5400
LSLLDSRWEA LLSRAEARNR QLEGISVVAQ EFHGTLEPLN EWLTAVEKKL ANSEPIGTQA 5460
PKLEEQISQH KALQEDILLR KQSVDQALLN GLELLKQTTG DEVLIIQDKL EAIKARYKDI 5520
TKLSADVAKT LEHALQLAGQ LQSMHKELCN WLDKVEVELL SYETQGLKGE AASQVQERQK 5580
ELKNEVRSNK ALVDSLNEVS SALLELVPCR AKEGLEKTIA DDNEPLPDCE PTQSRHKVEE 5640
IDAAILRSQQ FEQAADAELS WITETQKKLM SLGDIRLEQD QTSAQLQVQK AFTMDILRHK 5700
DIIDELVTSG HKIMTTSGEE EKQSMKKKLD KVLKKYDAVC QINSERHLQL ERAQSLVSQF 5760
WETYEELWPW LTETQRIISQ LPAPALEYET FERQQEEHRQ LRELIAEHKP HIDKMNKTGP 5820
QLLELSPKEG IYIQEKYVAA DTLYSQIKED VKKRAVVLDE AISQSTQFHD KIDQILESLE 5880
RIAERLRQPP SISAEVEKIK EQIGENKSVS VDMEKLQPLY ETLRQRGEEM IARSEGTEKD 5940
VSARAVQDKL DQMVFIWGSI HTLVEEREAK LLDVMELAEK FWCDHMSLVV TIKDTQDFIR 6000
DLEDPGIDPS VVKQQQEAAE AIREEIDGLQ EELDMVITLG SELIAACGEP DKPIVKKSID 6060
ELNSAWDSLN KAWKDRVDRL EEAMQAAVQY QDGLQGIFDW VDIAGDKLAT MSPIGTDLET 6120
VKQQIEELKQ FKSEAYQQQM EMERLNHQAE LLLKKVTEEA DKHTVQDPLM ELKLIWDSLD 6180
ERIVSRQHKL EGTLLALGQF QHALDELLAW LTHTKGLLSE QKPVGGDPKA IEIELAKHHV 6240
LQNDVLAHQS TVEAVNKAGN DLIESSEGEE ASNLQYKLRI LNQRWQDILE KTDQRKQQLD 6300
SALRQAKGFH GEIEDLQQWL TDTERHLLAS KPLGGLPETA KEQLNAHMEV CTAFAIKEET 6360
YKSLMLRGQQ MLARCPRSAE TNIDQDITNL KEKWESVKSK LNEKKTKLEE ALHLAMNFHN 6420
SLQDFINWLT QAEQTLNVAS RPSLILDTIL FQIDEHKVFA NEVNSHREQI IELDKTGTHL 6480
KYFSQKQDVV LIKNLLISVQ SRWEKVVQRL VERGRSLDEA RKRAKQFHEA WSKLMEWLEE 6540
SEKSLDSELE IANDPDKIKA QLVQHKEFQK SLGGKHSVYD TTNRTGRSLK EKTSLADDNL 6600
KLDNMLSELR DKWDTICGKS VERQNKLEEA LLFSGQFTDA LQALIDWLYR VEPQLAEDQP 6660
VHGDIDLVMS LIDNHKVFQK ELGKRTSSVQ ALKRSARELI EGSRDDSSWV RVQMQELSTR 6720
WETVCALSIS KQTRLESALQ QAEEFHSVVH TLLEWLAEAE QTLRFHGALP DDEDALRTLI 6780
EQHKEFMKRL EEKRAELSKA TGMGDALLAV CHPDSITTIK HWITIIQARF EEVLAWAKQH 6840
QQRLAGALAG LIAKQELLET LLAWLQWAET TLTEKDKEVI PQEIEEVKTL IAEHQTFMEE 6900
MTRKQPDVDK VTKTYKRRAT DPPSLQSHIP VLDKGRAGRK RFPASGFYPS GSQTQIETKN 6960
PRVNLLVSKW QQVWLLALER RRKLNDALDR LEELREFANF DFDIWRKKYM RWMNHKKSRV 7020
MDFFRRIDKD QDGKITRQEF IDGILSSKFP TSRLEMSAVA DIFDRDGDGY IDYYEFVAAL 7080
HPNKDAYKPI TDADKIGDEV TRQVAKCKCA KRFQVEQIGD NKYRFFLGNQ FGDSQQLRLV 7140
RILRSTVMVR VGGGWMALDE FLVKNDPCRA KGRTNMELRE KFILADGASQ GMAAFRPRGR 7200
RSRPSSRGAS PNRSTSGSSH ACQAASPPVP AAASTPKILH PLTRNYGKPW LANSKMSTPC 7260
KAAECPDFPV SSAEGTPIQG SKLRLPGYLS GKGFHSGEDS ALITTAAARV RTQFAESRKT 7320
PSRPGSRAGS KAGSRASSRR GSDASDFDIS EIQSVCSDVE TVPQTHRPVP RAGSRPSTAK 7380
PSKIPTPQRR SPASKLDKSS KR 7402 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:MGI.
 GO:0030424; C:axon; IEA:UniProtKB-SubCell.
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; ISO:MGI.
 GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0005925; C:focal adhesion; IDA:UniProtKB.
 GO:0031673; C:H zone; IDA:UniProtKB.
 GO:0030056; C:hemidesmosome; IDA:MGI.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0014704; C:intercalated disc; IDA:UniProtKB.
 GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
 GO:0009898; C:internal side of plasma membrane; IDA:UniProtKB.
 GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
 GO:0035371; C:microtubule plus end; ISS:UniProtKB.
 GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
 GO:0005635; C:nuclear envelope; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
 GO:0042383; C:sarcolemma; IDA:UniProtKB.
 GO:0001725; C:stress fiber; IDA:UniProtKB.
 GO:0030018; C:Z disc; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0007409; P:axonogenesis; IMP:MGI.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0007050; P:cell cycle arrest; IEA:InterPro.
 GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.
 GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
 GO:0046907; P:intracellular transport; IDA:UniProtKB.
 GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:MGI.
 GO:0008090; P:retrograde axon cargo transport; IMP:MGI. 
Interpro
 IPR001589; Actinin_actin-bd_CS.
 IPR001715; CH-domain.
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR003108; GAS2_dom.
 IPR001101; Plectin_repeat.
 IPR018159; Spectrin/alpha-actinin.
 IPR002017; Spectrin_repeat. 
Pfam
 PF00307; CH
 PF13499; EF_hand_5
 PF02187; GAS2
 PF00681; Plectin
 PF00435; Spectrin 
SMART
 SM00033; CH
 SM00054; EFh
 SM00243; GAS2
 SM00250; PLEC
 SM00150; SPEC 
PROSITE
 PS00019; ACTININ_1
 PS00020; ACTININ_2
 PS50021; CH
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS51460; GAR
 PS50002; SH3 
PRINTS