CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023276
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 
Protein Synonyms/Alias
 620 kDa actin-binding protein; ABP620; Actin cross-linking family protein 7; Macrophin-1; Trabeculin-alpha 
Gene Name
 MACF1 
Gene Synonyms/Alias
 ABP620; ACF7; KIAA0465; KIAA1251 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51VQKKTFTKWVNKHLMubiquitination[1]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Isoform 2 is a F-actin-binding protein which may play a role in cross-linking actin to other cytoskeletal proteins and also binds to microtubules. Plays an important role in ERBB2- dependent stabilization of microtubules at the cell cortex. Acts as a positive regulator of Wnt receptor signaling pathway and is involved in the translocation of AXIN1 and its associated complex (composed of APC, CTNNB1 and GSK3B) from the cytoplasm to the cell membrane. Has actin-regulated ATPase activity and is essential for controlling focal adhesions (FAs) assembly and dynamics. May play role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with GOLGA4. Plays a key role in wound healing and epidermal cell migration. Required for efficient upward migration of bulge cells in response to wounding and this function is primarily rooted in its ability to coordinate MT dynamics and polarize hair follicle stem cells (By similarity). 
Sequence Annotation
 DOMAIN 1 295 Actin-binding.
 DOMAIN 78 181 CH 1.
 REPEAT 148 171 LRR 1.
 DOMAIN 194 295 CH 2.
 REPEAT 240 264 LRR 2.
 REPEAT 377 399 LRR 3.
 REPEAT 441 464 LRR 4.
 DOMAIN 871 923 SH3.
 REPEAT 1050 1073 LRR 5.
 REPEAT 1128 1154 LRR 6.
 REPEAT 1187 1210 LRR 7.
 REPEAT 1257 1282 LRR 8.
 REPEAT 1577 1621 Plectin 1.
 REPEAT 1654 1696 Plectin 2.
 REPEAT 1769 1809 Plectin 3.
 REPEAT 1811 1848 Plectin 4.
 REPEAT 1855 1886 Plectin 5.
 REPEAT 2290 2332 Plectin 6.
 REPEAT 2367 2410 Plectin 7.
 REPEAT 2411 2437 Plectin 8.
 REPEAT 2501 2543 Plectin 9.
 REPEAT 2581 2612 Plectin 10.
 REPEAT 2686 2730 Plectin 11.
 REPEAT 3239 3262 LRR 9.
 REPEAT 3264 3283 LRR 10.
 REPEAT 3646 3669 LRR 11.
 REPEAT 3696 3720 LRR 12.
 REPEAT 3883 3957 Spectrin 1.
 REPEAT 3936 3958 LRR 13.
 REPEAT 4000 4108 Spectrin 2.
 REPEAT 4125 4150 LRR 14.
 REPEAT 4261 4287 LRR 15.
 REPEAT 4466 4574 Spectrin 3.
 REPEAT 4511 4534 LRR 16.
 REPEAT 4601 4624 LRR 17.
 REPEAT 4769 4792 LRR 18.
 REPEAT 4800 4904 Spectrin 4.
 REPEAT 4909 5012 Spectrin 5.
 REPEAT 5051 5076 LRR 19.
 REPEAT 5172 5194 LRR 20.
 REPEAT 5236 5341 Spectrin 6.
 REPEAT 5281 5304 LRR 21.
 REPEAT 5348 5450 Spectrin 7.
 REPEAT 5455 5557 Spectrin 8.
 REPEAT 5695 5719 LRR 22.
 REPEAT 5783 5885 Spectrin 9.
 REPEAT 5804 5828 LRR 23.
 REPEAT 6005 6110 Spectrin 10.
 REPEAT 6115 6219 Spectrin 11.
 REPEAT 6225 6328 Spectrin 12.
 REPEAT 6333 6439 Spectrin 13.
 REPEAT 6443 6547 Spectrin 14.
 REPEAT 6496 6519 LRR 24.
 REPEAT 6552 6658 Spectrin 15.
 REPEAT 6665 6766 Spectrin 16.
 REPEAT 6771 6874 Spectrin 17.
 DOMAIN 7041 7076 EF-hand 1.
 DOMAIN 7077 7112 EF-hand 2.
 DOMAIN 7117 7189 GAR.
 REGION 7117 7388 C-terminal tail (By similarity).
 REGION 7313 7328 4 X 4 AA tandem repeats of [GS]-S-R-[AR].
 MOD_RES 280 280 Phosphoserine.
 MOD_RES 1376 1376 Phosphoserine.
 MOD_RES 3927 3927 Phosphoserine.
 MOD_RES 4495 4495 Phosphoserine.
 MOD_RES 4496 4496 Phosphoserine.
 MOD_RES 4521 4521 Phosphoserine.
 MOD_RES 4962 4962 Phosphoserine.
 MOD_RES 6032 6032 Phosphoserine (By similarity).
 MOD_RES 6210 6210 N6-acetyllysine.
 MOD_RES 6967 6967 Phosphoserine.
 MOD_RES 7254 7254 Phosphothreonine.
 MOD_RES 7292 7292 Phosphoserine.
 MOD_RES 7330 7330 Phosphoserine.
 MOD_RES 7333 7333 Phosphoserine (By similarity).  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Calcium; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Golgi apparatus; Leucine-rich repeat; Membrane; Metal-binding; Microtubule; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 7388 AA 
Protein Sequence
MFPVLWAGIP GRDVGSLQPL PPGFKQFCTS ASRVAVIADE RDRVQKKTFT KWVNKHLMKV 60
RKHINDLYED LRDGHNLISL LEVLSGIKLP REKGRMRFHR LQNVQIALDF LKQRQVKLVN 120
IRNDDITDGN PKLTLGLIWT IILHFQISDI YISGESGDMS AKEKLLLWTQ KVTAGYTGIK 180
CTNFSSCWSD GKMFNALIHR YRPDLVDMER VQIQSNRENL EQAFEVAERL GVTRLLDAED 240
VDVPSPDEKS VITYVSSIYD AFPKVPEGGE GISATEVDSR WQEYQSRVDS LIPWIKQHTI 300
LMSDKTFPQN PVELKALYNQ YIHFKETEIL AKEREKGRIE ELYKLLEVWI EFGRIKLPQG 360
YHPNDVEEEW GKLIIEMLER EKSLRPAVER LELLLQIANK IQNGALNCEE KLTLAKNTLQ 420
ADAAHLESGQ PVQCESDVIM YIQECEGLIR QLQVDLQILR DENYYQLEEL AFRVMRLQDE 480
LVTLRLECTN LYRKGHFTSL ELVPPSTLTT THLKAEPLTK ATHSSSTSWF RKPMTRAELV 540
AISSSEDEGN LRFVYELLSW VEEMQMKLER AEWGNDLPSV ELQLETQQHI HTSVEELGSS 600
VKEARLYEGK MSQNFHTSYA ETLGKLETQY CKLKETSSFR MRHLQSLHKF VSRATAELIW 660
LNEKEEEELA YDWSDNNSNI SAKRNYFSEL TMELEEKQDV FRSLQDTAEL LSLENHPAKQ 720
TVEAYSAAVQ SQLQWMKQLC LCVEQHVKEN TAYFQFFSDA RELESFLRNL QDSIKRKYSC 780
DHNTSLSRLE DLLQDSMDEK EQLIQSKSSV ASLVGRSKTI VQLKPRSPDH VLKNTISVKA 840
VCDYRQIEIT ICKNDECVLE DNSQRTKWKV ISPTGNEAMV PSVCFLIPPP NKDAIEMASR 900
VEQSYQKVMA LWHQLHVNTK SLISWNYLRK DLDLVQTWNL EKLRSSAPGE CHQIMKNLQA 960
HYEDFLQDSR DSVLFSVADR LRLEEEVEAC KARFQHLMKS MENEDKEETV AKMYISELKN 1020
IRLRLEEYEQ RVVKRIQSLA SSRTDRDAWQ DNALRIAEQE HTQEDLQQLR SDLDAVSMKC 1080
DSFLHQSPSS SSVPTLRSEL NLLVEKMDHV YGLSTVYLNK LKTVDVIVRS IQDAELLVKG 1140
YEIKLSQEEV VLADLSALEA HWSTLRHWLS DVKDKNSVFS VLDEEIAKAK VVAEQMSRLT 1200
PERNLDLERY QEKGSQLQER WHRVIAQLEI RQSELESIQE VLGDYRACHG TLIKWIEETT 1260
AQQEMMKPGQ AEDSRVLSEQ LSQQTALFAE IERNQTKLDQ CQKFSQQYST IVKDYELQLM 1320
TYKAFVESQQ KSPGKRRRML SSSDAITQEF MDLRTRYTAL VTLTTQHVKY ISDALRRLEE 1380
EEKVVEEEKQ EHVEKVKELL GWVSTLARNT QGKATSSETK ESTDIEKAIL EQQVLSEELT 1440
TKKEQVSEAI KTSQIFLAKH GHKLSEKEKK QISEQLNALN KAYHDLCDGS ANQLQQLQSQ 1500
LAHQTEQKTL QKQQNTCHQQ LEDLCSWVGQ AERALAGHQG RTTQQDLSAL QKNQSDLKDL 1560
QDDIQNRATS FATVVKDIEG FMEENQTKLS PRELTALREK LHQAKEQYEA LQEETRVAQK 1620
ELEEAVTSAL QQETEKSKAA KELAENKKKI DALLDWVTSV GSSGGQLLTN LPGMEQLSGA 1680
SLEKGALDTT DGYMGVNQAP EKLDKQCEMM KARHQELLSQ QQNFILATQS AQAFLDQHGH 1740
NLTPEEQQML QQKLGELKEQ YSTSLAQSEA ELKQVQTLQD ELQKFLQDHK EFESWLERSE 1800
KELENMHKGG SSPETLPSLL KRQGSFSEDV ISHKGDLRFV TISGQKVLDM ENSFKEGKEP 1860
SEIGNLVKDK LKDATERYTA LHSKCTRLGS HLNMLLGQYH QFQNSADSLQ AWMQACEANV 1920
EKLLSDTVAS DPGVLQEQLA TTKQLQEELA EHQVPVEKLQ KVARDIMEIE GEPAPDHRHV 1980
QETTDSILSH FQSLSYSLAE RSSLLQKAIA QSQSVQESLE SLLQSIGEVE QNLEGKQVSS 2040
LSSGVIQEAL ATNMKLKQDI ARQKSSLEAT REMVTRFMET ADSTTAAVLQ GKLAEVSQRF 2100
EQLCLQQQEK ESSLKKLLPQ AEMFEHLSGK LQQFMENKSR MLASGNQPDQ DITHFFQQIQ 2160
ELNLEMEDQQ ENLDTLEHLV TELSSCGFAL DLCQHQDRVQ NLRKDFTELQ KTVKEREKDA 2220
SSCQEQLDEF RKLVRTFQKW LKETEGSIPP TETSMSAKEL EKQIEHLKSL LDDWASKGTL 2280
VEEINCKGTS LENLIMEITA PDSQGKTDLT EIQCDMSDVN LKYEKLGGVL HERQESLQAI 2340
LNRMEEVHKE ANSVLQWLES KEEVLKSMDA MSSPTKTETV KAQAESNKAF LAELEQNSPK 2400
IQKVKEALAG LLVTYPNSQE AENWKKIQEE LNSRWERATE VTVARQRQLE ESASHLACFQ 2460
AAESQLRPWL MEKELMMGVL GPLSIDPNML NAQKQQVQFM LKEFEARRQQ HEQLNEAAQG 2520
ILTGPGDVSL STSQVQKELQ SINQKWVELT DKLNSRSSQI DQAIVKSTQY QELLQDLSEK 2580
VRAVGQRLSV QSAISTQPEA VKQQLEETSE IRSDLEQLDH EVKEAQTLCD ELSVLIGEQY 2640
LKDELKKRLE TVALPLQGLE DLAADRINRL QAALASTQQF QQMFDELRTW LDDKQSQQAK 2700
NCPISAKLER LQSQLQENEE FQKSLNQHSG SYEVIVAEGE SLLLSVPPGE EKRTLQNQLV 2760
ELKNHWEELS KKTADRQSRL KDCMQKAQKY QWHVEDLVPW IEDCKAKMSE LRVTLDPVQL 2820
ESSLLRSKAM LNEVEKRRSL LEILNSAADI LINSSEADED GIRDEKAGIN QNMDAVTEEL 2880
QAKTGSLEEM TQRLREFQES FKNIEKKVEG AKHQLEIFDA LGSQACSNKN LEKLRAQQEV 2940
LQALEPQVDY LRNFTQGLVE DAPDGSDASQ LLHQAEVAQQ EFLEVKQRVN SGCVMMENKL 3000
EGIGQFHCRV REMFSQLADL DDELDGMGAI GRDTDSLQSQ IEDVRLFLNK IHVLKLDIEA 3060
SEAECRHMLE EEGTLDLLGL KRELEALNKQ CGKLTERGKA RQEQLELTLG RVEDFYRKLK 3120
GLNDATTAAE EAEALQWVVG TEVEIINQQL ADFKMFQKEQ VDPLQMKLQQ VNGLGQGLIQ 3180
SAGKDCDVQG LEHDMEEINA RWNTLNKKVA QRIAQLQEAL LHCGKFQDAL EPLLSWLADT 3240
EELIANQKPP SAEYKVVKAQ IQEQKLLQRL LDDRKATVDM LQAEGGRIAQ SAELADREKI 3300
TGQLESLESR WTELLSKAAA RQKQLEDILV LAKQFHETAE PISDFLSVTE KKLANSEPVG 3360
TQTAKIQQQI IRHKALEEDI ENHATDVHQA VKIGQSLSSL TSPAEQGVLS EKIDSLQARY 3420
SEIQDRCCRK AALLDQALSN ARLFGEDEVE VLNWLAEVED KLSSVFVKDF KQDVLHRQHA 3480
DHLALNEEIV NRKKNVDQAI KNGQALLKQT TGEEVLLIQE KLDGIKTRYA DITVTSSKAL 3540
RTLEQARQLA TKFQSTYEEL TGWLREVEEE LATSGGQSPT GEQIPQFQQR QKELKKEVME 3600
HRLVLDTVNE VSRALLELVP WRAREGLDKL VSDANEQYKL VSDTIGQRVD EIDAAIQRSQ 3660
QYEQAADAEL AWVAETKRKL MALGPIRLEQ DQTTAQLQVQ KAFSIDIIRH KDSMDELFSH 3720
RSEIFGTCGE EQKTVLQEKT ESLIQQYEAI SLLNSERYAR LERAQVLVNQ FWETYEELSP 3780
WIEETRALIA QLPSPAIDHE QLRQQQEEMR QLRESIAEHK PHIDKLLKIG PQLKELNPEE 3840
GEMVEEKYQK AENMYAQIKE EVRQRALALD EAVSQSTQIT EFHDKIEPML ETLENLSSRL 3900
RMPPLIPAEV DKIRECISDN KSATVELEKL QPSFEALKRR GEELIGRSQG ADKDLAAKEI 3960
QDKLDQMVFF WEDIKARAEE REIKFLDVLE LAEKFWYDMA ALLTTIKDTQ DIVHDLESPG 4020
IDPSIIKQQV EAAETIKEET DGLHEELEFI RILGADLIFA CGETEKPEVR KSIDEMNNAW 4080
ENLNKTWKER LEKLEDAMQA AVQYQDTLQA MFDWLDNTVI KLCTMPPVGT DLNTVKDQLN 4140
EMKEFKVEVY QQQIEMEKLN HQGELMLKKA TDETDRDIIR EPLTELKHLW ENLGEKIAHR 4200
QHKLEGALLA LGQFQHALEE LMSWLTHTEE LLDAQRPISG DPKVIEVELA KHHVLKNDVL 4260
AHQATVETVN KAGNELLESS AGDDASSLRS RLEAMNQCWE SVLQKTEERE QQLQSTLQQA 4320
QGFHSEIEDF LLELTRMESQ LSASKPTGGL PETAREQLDT HMELYSQLKA KEETYNQLLD 4380
KGRLMLLSRD DSGSGSKTEQ SVALLEQKWH VVSSKMEERK SKLEEALNLA TEFQNSLQEF 4440
INWLTLAEQS LNIASPPSLI LNTVLSQIEE HKVFANEVNA HRDQIIELDQ TGNQLKFLSQ 4500
KQDVVLIKNL LVSVQSRWEK VVQRSIERGR SLDDARKRAK QFHEAWKKLI DWLEDAESHL 4560
DSELEISNDP DKIKLQLSKH KEFQKTLGGK QPVYDTTIRT GRALKEKTLL PEDSQKLDNF 4620
LGEVRDKWDT VCGKSVERQH KLEEALLFSG QFMDALQALV DWLYKVEPQL AEDQPVHGDL 4680
DLVMNLMDAH KVFQKELGKR TGTVQVLKRS GRELIENSRD DTTWVKGQLQ ELSTRWDTVC 4740
KLSVSKQSRL EQALKQAEVF RDTVHMLLEW LSEAEQTLRF RGALPDDTEA LQSLIDTHKE 4800
FMKKVEEKRV DVNSAVAMGE VILAVCHPDC ITTIKHWITI IRARFEEVLT WAKQHQQRLE 4860
TALSELVANA ELLEELLAWI QWAETTLIQR DQEPIPQNID RVKALIAEHQ TFMEEMTRKQ 4920
PDVDRVTKTY KRKNIEPTHA PFIEKSRSGG RKSLSQPTPP PMPILSQSEA KNPRINQLSA 4980
RWQQVWLLAL ERQRKLNDAL DRLEELKEFA NFDFDVWRKK YMRWMNHKKS RVMDFFRRID 5040
KDQDGKITRQ EFIDGILASK FPTTKLEMTA VADIFDRDGD GYIDYYEFVA ALHPNKDAYR 5100
PTTDADKIED EVTRQVAQCK CAKRFQVEQI GENKYRFGDS QQLRLVRILR STVMVRVGGG 5160
WMALDEFLVK NDPCRARGRT NIELREKFIL PEGASQGMTP FRSRGRRSKP SSRAASPTRS 5220
SSSASQSNHS CTSMPSSPAT PASGTKVIPS SGSKLKRPTP TFHSSRTSLA GDTSNSSSPA 5280
STGAKTNRAD PKKSASRPGS RAGSRAGSRA SSRRGSDASD FDLLETQSAC SDTSESSAAG 5340
GQGNSRRGLN KPSKIPTMSK KTTTASPRTP GPKR 5374 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0005874; C:microtubule; IDA:UniProtKB.
 GO:0032587; C:ruffle membrane; IDA:UniProtKB.
 GO:0051015; F:actin filament binding; NAS:UniProtKB.
 GO:0016887; F:ATPase activity; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO:0008017; F:microtubule binding; NAS:UniProtKB.
 GO:0007050; P:cell cycle arrest; IEA:InterPro.
 GO:0006928; P:cellular component movement; IEA:Compara.
 GO:0007163; P:establishment or maintenance of cell polarity; IEA:Compara.
 GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
 GO:0001707; P:mesoderm formation; IEA:Compara.
 GO:0030177; P:positive regulation of Wnt receptor signaling pathway; ISS:UniProtKB.
 GO:0006620; P:posttranslational protein targeting to membrane; IEA:Compara.
 GO:0010632; P:regulation of epithelial cell migration; ISS:UniProtKB.
 GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
 GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
 GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
 GO:0042060; P:wound healing; ISS:UniProtKB. 
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