CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011016
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dystonin 
Protein Synonyms/Alias
 230 kDa bullous pemphigoid antigen; 230/240 kDa bullous pemphigoid antigen; Bullous pemphigoid antigen 1; BPA; Bullous pemphigoid antigen; Dystonia musculorum protein; Hemidesmosomal plaque protein 
Gene Name
 DST 
Gene Synonyms/Alias
 BP230; BP240; BPAG1; DMH; DT; KIAA0728 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5470AEPADKVKILKQLSLubiquitination[1, 2]
Reference
 [1] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [2] 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
 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. 
Sequence Annotation
 DOMAIN 35 252 Actin-binding.
 DOMAIN 35 138 CH 1.
 DOMAIN 151 252 CH 2.
 REPEAT 701 797 Spectrin 1.
 DOMAIN 890 942 SH3.
 REPEAT 1584 1626 Plectin 1.
 REPEAT 1660 1703 Plectin 2.
 REPEAT 1774 1817 Plectin 3.
 REPEAT 1818 1855 Plectin 4.
 REPEAT 1856 1891 Plectin 5.
 REPEAT 3924 4000 Spectrin 2.
 REPEAT 4069 4153 Spectrin 3.
 REPEAT 4514 4622 Spectrin 4.
 REPEAT 4626 4731 Spectrin 5.
 REPEAT 4849 4952 Spectrin 6.
 REPEAT 5281 5389 Spectrin 7.
 REPEAT 5396 5497 Spectrin 8.
 REPEAT 5504 5606 Spectrin 9.
 REPEAT 5829 5933 Spectrin 10.
 REPEAT 5940 6042 Spectrin 11.
 REPEAT 6048 6154 Spectrin 12.
 REPEAT 6184 6264 Spectrin 13.
 REPEAT 6270 6373 Spectrin 14.
 REPEAT 6379 6481 Spectrin 15.
 REPEAT 6490 6592 Spectrin 16.
 REPEAT 6597 6700 Spectrin 17.
 REPEAT 6705 6811 Spectrin 18.
 REPEAT 6818 6918 Spectrin 19.
 REPEAT 6923 7026 Spectrin 20.
 DOMAIN 7197 7232 EF-hand 1.
 DOMAIN 7233 7268 EF-hand 2.
 DOMAIN 7273 7351 GAR.
 MOTIF 1383 1389 Nuclear localization signal; in isoform 6
 MOTIF 7550 7553 Microtubule tip localization signal.
 MOD_RES 2919 2919 Phosphoserine.
 MOD_RES 7364 7364 Phosphoserine (By similarity).
 MOD_RES 7432 7432 Phosphoserine.
 CROSSLNK 5470 5470 Glycyl lysine isopeptide (Lys-Gly)  
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; Endoplasmic reticulum; Intermediate filament; Isopeptide bond; Lipoprotein; Membrane; Metal-binding; Microtubule; Muscle protein; Neuropathy; Nucleus; Palmitate; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain; Transmembrane; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 7570 AA 
Protein Sequence
MAGYLSPAAY LYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY 60
EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD 120
GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG IRCENFTTCW 180
RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE 240
KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VTTMSERTFP 300
NNPVELKALY NQYLQFKETE IPPKETEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK 360
EWGKLIIAML EREKALRPEV ERLEMLQQIA NRVQRDSVIC EDKLILAGNA LQSDSKRLES 420
GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC 480
SSVYSKGRIL TTEQTKLMIS GITQSLNSGF AQTLHPSLTS GLTQSLTPSL TSSSMTSGLS 540
SGMTSRLTPS VTPAYTPGFP SGLVPNFSSG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE 600
EEINMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI 660
SEIQMTAPLK LTYAEKLHRL ESQYAKLLNT SRNQERHLDT LHNFVSRATN ELIWLNEKEE 720
EEVAYDWSER NTNIARKKDY HAELMRELDQ KEENIKSVQE IAEQLLLENH PARLTIEAYR 780
AAMQTQWSWI LQLCQCVEQH IKENTAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI 840
HKLEDLVQES MEEKEELLQY KSTIANLMGK AKTIIQLKPR NSDCPLKTSI PIKAICDYRQ 900
IEITIYKDDE CVLANNSHRA KWKVISPTGN EAMVPSVCFT VPPPNKEAVD LANRIEQQYQ 960
NVLTLWHESH INMKSVVSWH YLINEIDRIR ASNVASIKTM LPGEHQQVLS NLQSRFEDFL 1020
EDSQESQVFS GSDITQLEKE VNVCKQYYQE LLKSAEREEQ EESVYNLYIS EVRNIRLRLE 1080
NCEDRLIRQI RTPLERDDLH ESVFRITEQE KLKKELERLK DDLGTITNKC EEFFSQAAAS 1140
SSVPTLRSEL NVVLQNMNQV YSMSSTYIDK LKTVNLVLKN TQAAEALVKL YETKLCEEEA 1200
VIADKNNIEN LISTLKQWRS EVDEKRQVFH ALEDELQKAK AISDEMFKTY KERDLDFDWH 1260
KEKADQLVER WQNVHVQIDN RLRDLEGIGK SLKYYRDTYH PLDDWIQQVE TTQRKIQENQ 1320
PENSKTLATQ LNQQKMLVSE IEMKQSKMDE CQKYAEQYSA TVKDYELQTM TYRAMVDSQQ 1380
KSPVKRRRMQ SSADLIIQEF MDLRTRYTAL VTLMTQYIKF AGDSLKRLEE EEKSLEEEKK 1440
EHVEKAKELQ KWVSNISKTL KDAEKAGKPP FSKQKISSEE ISTKKEQLSE ALQTIQLFLA 1500
KHGDKMTDEE RNELEKQVKT LQESYNLLFS ESLKQLQESQ TSGDVKVEEK LDKVIAGTID 1560
QTTGEVLSVF QAVLRGLIDY DTGIRLLETQ LMISGLISPE LRKCFDLKDA KSHGLIDEQI 1620
LCQLKELSKA KEIISAASPT TIPVLDALAQ SMITESMAIK VLEILLSTGS LVIPATGEQL 1680
TLQKAFQQNL VSSALFSKVL ERQNMCKDLI DPCTSEKVSL IDMVQRSTLQ ENTGMWLLPV 1740
RPQEGGRITL KCGRNISILR AAHEGLIDRE TMFRLLSAQL LSGGLINSNS GQRMTVEEAV 1800
REGVIDRDTA SSILTYQVQT GGIIQSNPAK RLTVDEAVQC DLITSSSALL VLEAQRGYVG 1860
LIWPHSGEIF PTSSSLQQEL ITNELAYKIL NGRQKIAALY IPESSQVIGL DAAKQLGIID 1920
NNTASILKNI TLPDKMPDLG DLEACKNARR WLSFCKFQPS TVHDYRQEED VFDGEEPVTT 1980
QTSEETKKLF LSYLMINSYM DANTGQRLLL YDGDLDEAVG MLLEGCHAEF DGNTAIKECL 2040
DVLSSSGVFL NNASGREKDE CTATPSSFNK CHCGEPEHEE TPENRKCAID EEFNEMRNTV 2100
INSEFSQSGK LASTISIDPK VNSSPSVCVP SLISYLTQTE LADISMLRSD SENILTNYEN 2160
QSRVETNERA NECSHSKNIQ NFPSDLIENP IMKSKMSKFC GVNETENEDN TNRDSPIFDY 2220
SPRLSALLSH DKLMHSQGSF NDTHTPESNG NKCEAPALSF SDKTMLSGQR IGEKFQDQFL 2280
GIAAINISLP GEQYGQKSLN MISSNPQVQY HNDKYISNTS GEDEKTHPGF QQMPEDKEDE 2340
SEIEEYSCAV TPGGDTDNAI VSLTCATPLL DETISASDYE TSLLNDQQNN TGTDTDSDDD 2400
FYDTPLFEDD DHDSLLLDGD DRDCLHPEDY DTLQEENDET ASPADVFYDV SKENENSMVP 2460
QGAPVGSLSV KNKAHCLQDF LMDVEKDELD SGEKIHLNPV GSDKVNGQSL ETGSERECTN 2520
ILEGDESDSL TDYDIVGGKE SFTASLKFDD SGSWRGRKEE YVTGQEFHSD TDHLDSMQSE 2580
ESYGDYIYDS NDQDDDDDDG IDEEGGGIRD ENGKPRCQNV AEDMDIQLCA SILNENSDEN 2640
ENINTMILLD KMHSCSSLEK QQRVNVVQLA SPSENNLVTE KSNLPEYTTE IAGKSKENLL 2700
NHEMVLKDVL PPIIKDTESE KTFGPASISH DNNNISSTSE LGTDLANTKV KLIQGSELPE 2760
LTDSVKGKDE YFKNMTPKVD SSLDHIICTE PDLIGKPAEE SHLSLIASVT DKDPQGNGSD 2820
LIKGRDGKSD ILIEDETSIQ KMYLGEGEVL VEGLVEEENR HLKLLPGKNT RDSFKLINSQ 2880
FPFPQITNNE ELNQKGSLKK ATVTLKDEPN NLQIIVSKSP VQFENLEEIF DTSVSKEISD 2940
DITSDITSWE GNTHFEESFT DGPEKELDLF TYLKHCAKNI KAKDVAKPNE DVPSHVLITA 3000
PPMKEHLQLG VNNTKEKSTS TQKDSPLNDM IQSNDLCSKE SISGGGTEIS QFTPESIEAT 3060
LSILSRKHVE DVGKNDFLQS ERCANGLGND NSSNTLNTDY SFLEINNKKE RIEQQLPKEQ 3120
ALSPRSQEKE VQIPELSQVF VEDVKDILKS RLKEGHMNPQ EVEEPSACAD TKILIQNLIK 3180
RITTSQLVNE ASTVPSDSQM SDSSGVSPMT NSSELKPESR DDPFCIGNLK SELLLNILKQ 3240
DQHSQKITGV FELMRELTHM EYDLEKRGIT SKVLPLQLEN IFYKLLADGY SEKIEHVGDF 3300
NQKACSTSEM MEEKPHILGD IKSKEGNYYS PNLETVKEIG LESSTVWAST LPRDEKLKDL 3360
CNDFPSHLEC TSGSKEMASG DSSTEQFSSE LQQCLQHTEK MHEYLTLLQD MKPPLDNQES 3420
LDNNLEALKN QLRQLETFEL GLAPIAVILR KDMKLAEEFL KSLPSDFPRG HVEELSISHQ 3480
SLKTAFSSLS NVSSERTKQI MLAIDSEMSK LAVSHEEFLH KLKSFSDWVS EKSKSVKDIE 3540
IVNVQDSEYV KKRLEFLKNV LKDLGHTKMQ LETTAFDVQF FISEYAQDLS PNQSKQLLRL 3600
LNTTQKCFLD VQESVTTQVE RLETQLHLEQ DLDDQKIVAE RQQEYKEKLQ GICDLLTQTE 3660
NRLIGHQEAF MIGDGTVELK KYQSKQEELQ KDMQGSAQAL AEVVKNTENF LKENGEKLSQ 3720
EDKALIEQKL NEAKIKCEQL NLKAEQSKKE LDKVVTTAIK EETEKVAAVK QLEESKTKIE 3780
NLLDWLSNVD KDSERAGTKH KQVIEQNGTH FQEGDGKSAI GEEDEVNGNL LETDVDGQVG 3840
TTQENLNQQY QKVKAQHEKI ISQHQAVIIA TQSAQVLLEK QGQYLSPEEK EKLQKNMKEL 3900
KVHYETALAE SEKKMKLTHS LQEELEKFDA DYTEFEHWLQ QSEQELENLE AGADDINGLM 3960
TKLKRQKSFS EDVISHKGDL RYITISGNRV LEAAKSCSKR DGGKVDTSAT HREVQRKLDH 4020
ATDRFRSLYS KCNVLGNNLK DLVDKYQHYE DASCGLLAGL QACEATASKH LSEPIAVDPK 4080
NLQRQLEETK ALQGQISSQQ VAVEKLKKTA EVLLDARGSL LPAKNDIQKT LDDIVGRYED 4140
LSKSVNERNE KLQITLTRSL SVQDGLDEML DWMGNVESSL KEQGQVPLNS TALQDIISKN 4200
IMLEQDIAGR QSSINAMNEK VKKFMETTDP STASSLQAKM KDLSARFSEA SHKHKETLAK 4260
MEELKTKVEL FENLSEKLQT FLETKTQALT EVDVPGKDVT ELSQYMQEST SEFLEHKKHL 4320
EVLHSLLKEI SSHGLPSDKA LVLEKTNNLS KKFKEMEDTI KEKKEAVTSC QEQLDAFQVL 4380
VKSLKSWIKE TTKKVPIVQP SFGAEDLGKS LEDTKKLQEK WSLKTPEIQK VNNSGISLCN 4440
LISAVTTPAK AIAAVKSGGA VLNGEGTATN TEEFWANKGL TSIKKDMTDI SHGYEDLGLL 4500
LKDKIAELNT KLSKLQKAQE ESSAMMQWLQ KMNKTATKWQ QTPAPTDTEA VKTQVEQNKS 4560
FEAELKQNVN KVQELKDKLT ELLEENPDTP EAPRWKQMLT EIDSKWQELN QLTIDRQQKL 4620
EESSNNLTQF QTVEAQLKQW LVEKELMVSV LGPLSIDPNM LNTQRQQVQI LLQEFATRKP 4680
QYEQLTAAGQ GILSRPGEDP SLRGIVKEQL AAVTQKWDSL TGQLSDRCDW IDQAIVKSTQ 4740
YQSLLRSLSD KLSDLDNKLS SSLAVSTHPD AMNQQLETAQ KMKQEIQQEK KQIKVAQALC 4800
EDLSALVKEE YLKAELSRQL EGILKSFKDV EQKAENHVQH LQSACASSHQ FQQMSRDFQA 4860
WLDTKKEEQN KSHPISAKLD VLESLIKDHK DFSKTLTAQS HMYEKTIAEG ENLLLKTQGS 4920
EKAALQLQLN TIKTNWDTFN KQVKERENKL KESLEKALKY KEQVETLWPW IDKCQNNLEE 4980
IKFCLDPAEG ENSIAKLKSL QKEMDQHFGM VELLNNTANS LLSVCEIDKE VVTDENKSLI 5040
QKVDMVTEQL HSKKFCLENM TQKFKEFQEV SKESKRQLQC AKEQLDIHDS LGSQAYSNKY 5100
LTMLQTQQKS LQALKHQVDL AKRLAQDLVV EASDSKGTSD VLLQVETIAQ EHSTLSQQVD 5160
EKCSFLETKL QGIGHFQNTI REMFSQFAEF DDELDSMAPV GRDAETLQKQ KETIKAFLKK 5220
LEALMASNDN ANKTCKMMLA TEETSPDLVG IKRDLEALSK QCNKLLDRAQ AREEQVEGTI 5280
KRLEEFYSKL KEFSILLQKA EEHEESQGPV GMETETINQQ LNMFKVFQKE EIEPLQGKQQ 5340
DVNWLGQGLI QSAAKSTSTQ GLEHDLDDVN ARWKTLNKKV AQRAAQLQEA LLHCGRFQDA 5400
LESLLSWMVD TEELVANQKP PSAEFKVVKA QIQEQKLLQR LLDDRKSTVE VIKREGEKIA 5460
TTAEPADKVK ILKQLSLLDS RWEALLNKAE TRNRQLEGIS VVAQQFHETL EPLNEWLTTI 5520
EKRLVNCEPI GTQASKLEEQ IAQHKALEDD IINHNKHLHQ AVSIGQSLKV LSSREDKDMV 5580
QSKLDFSQVW YIEIQEKSHS RSELLQQALC NAKIFGEDEV ELMNWLNEVH DKLSKLSVQD 5640
YSTEGLWKQQ SELRVLQEDI LLRKQNVDQA LLNGLELLKQ TTGDEVLIIQ DKLEAIKARY 5700
KDITKLSTDV AKTLEQALQL ARRLHSTHEE LCTWLDKVEV ELLSYETQVL KGEEASQAQM 5760
RPKELKKEAK NNKALLDSLN EVSSALLELV PWRAREGLEK MVAEDNERYR LVSDTITQKV 5820
EEIDAAILRS QQFDQAADAE LSWITETEKK LMSLGDIRLE QDQTSAQLQV QKTFTMEILR 5880
HKDIIDDLVK SGHKIMTACS EEEKQSMKKK LDKVLKNYDT ICQINSERYL QLERAQSLVN 5940
QFWETYEELW PWLTETQSII SQLPAPALEY ETLRQQQEEH RQLRELIAEH KPHIDKMNKT 6000
GPQLLELSPG EGFSIQEKYV AADTLYSQIK EDVKKRAVAL DEAISQSTQF HDKIDQILES 6060
LERIVERLRQ PPSISAEVEK IKEQISENKN VSVDMEKLQP LYETLKQRGE EMIARSGGTD 6120
KDISAKAVQD KLDQMVFIWE NIHTLVEERE AKLLDVMELA EKFWCDHMSL IVTIKDTQDF 6180
IRDLEDPGID PSVVKQQQEA AETIREEIDG LQEELDIVIN LGSELIAACG EPDKPIVKKS 6240
IDELNSAWDS LNKAWKDRID KLEEAMQAAV QYQDGLQAVF DWVDIAGGKL ASMSPIGTDL 6300
ETVKQQIEEL KQFKSEAYQQ QIEMERLNHQ AELLLKKVTE ESDKHTVQDP LMELKLIWDS 6360
LEERIINRQH KLEGALLALG QFQHALDELL AWLTHTEGLL SEQKPVGGDP KAIEIELAKH 6420
HVLQNDVLAH QSTVEAVNKA GNDLIESSAG EEASNLQNKL EVLNQRWQNV LEKTEQRKQQ 6480
LDGALRQAKG FHGEIEDLQQ WLTDTERHLL ASKPLGGLPE TAKEQLNVHM EVCAAFEAKE 6540
ETYKSLMQKG QQMLARCPKS AETNIDQDIN NLKEKWESVE TKLNERKTKL EEALNLAMEF 6600
HNSLQDFINW LTQAEQTLNV ASRPSLILDT VLFQIDEHKV FANEVNSHRE QIIELDKTGT 6660
HLKYFSQKQD VVLIKNLLIS VQSRWEKVVQ RLVERGRSLD DARKRAKQFH EAWSKLMEWL 6720
EESEKSLDSE LEIANDPDKI KTQLAQHKEF QKSLGAKHSV YDTTNRTGRS LKEKTSLADD 6780
NLKLDDMLSE LRDKWDTICG KSVERQNKLE EALLFSGQFT DALQALIDWL YRVEPQLAED 6840
QPVHGDIDLV MNLIDNHKAF QKELGKRTSS VQALKRSARE LIEGSRDDSS WVKVQMQELS 6900
TRWETVCALS ISKQTRLEAA LRQAEEFHSV VHALLEWLAE AEQTLRFHGV LPDDEDALRT 6960
LIDQHKEFMK KLEEKRAELN KATTMGDTVL AICHPDSITT IKHWITIIRA RFEEVLAWAK 7020
QHQQRLASAL AGLIAKQELL EALLAWLQWA ETTLTDKDKE VIPQEIEEVK ALIAEHQTFM 7080
EEMTRKQPDV DKVTKTYKRR AADPSSLQSH IPVLDKGRAG RKRFPASSLY PSGSQTQIET 7140
KNPRVNLLVS KWQQVWLLAL ERRRKLNDAL DRLEELREFA NFDFDIWRKK YMRWMNHKKS 7200
RVMDFFRRID KDQDGKITRQ EFIDGILSSK FPTSRLEMSA VADIFDRDGD GYIDYYEFVA 7260
ALHPNKDAYK PITDADKIED EVTRQVAKCK CAKRFQVEQI GDNKYRFFLG NQFGDSQQLR 7320
LVRILRSTVM VRVGGGWMAL DEFLVKNDPC RVHHHGSKML RSESNSSITT TQPTIAKGRT 7380
NMELREKFIL ADGASQGMAA FRPRGRRSRP SSRGASPNRS TSVSSQAAQA ASPQVPATTT 7440
PKGTPIQGSK LRLPGYLSGK GFHSGEDSGL ITTAAARVRT QFADSKKTPS RPGSRAGSKA 7500
GSRASSRRGS DASDFDISEI QSVCSDVETV PQTHRPTPRA GSRPSTAKPS KIPTPQRKSP 7560
ASKLDKSSKR 7570 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
 GO:0030424; C:axon; IEA:UniProtKB-SubCell.
 GO:0033267; C:axon part; IDA:UniProtKB.
 GO:0009925; C:basal plasma membrane; NAS:UniProtKB.
 GO:0005604; C:basement membrane; TAS:ProtInc.
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0031252; C:cell leading edge; IDA:UniProtKB.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0031673; C:H zone; IEA:UniProtKB-SubCell.
 GO:0030056; C:hemidesmosome; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
 GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
 GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
 GO:0035371; C:microtubule plus end; IDA:UniProtKB.
 GO:0060053; C:neurofilament cytoskeleton; IEA:Compara.
 GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0030018; C:Z disc; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0007409; P:axonogenesis; IEA:Compara.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0007050; P:cell cycle arrest; IEA:InterPro.
 GO:0048870; P:cell motility; IMP:UniProtKB.
 GO:0031122; P:cytoplasmic microtubule organization; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB.
 GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
 GO:0045104; P:intermediate filament cytoskeleton organization; IEP:UniProtKB.
 GO:0030011; P:maintenance of cell polarity; IMP:UniProtKB.
 GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
 GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:Compara.
 GO:0009611; P:response to wounding; IDA:UniProtKB.
 GO:0008090; P:retrograde axon cargo transport; IEA:Compara. 
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