CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023275
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
2239DRVQNLRKDFTELQKubiquitination[1]
Reference
 [1] 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
 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
MSSSDEETLS ERSCRSERSC RSERSYRSER SGSLSPCPPG DTLPWNLPLH EQKKRKSQDS 60
VLDPAERAVV RVADERDRVQ KKTFTKWVNK HLMKVRKHIN DLYEDLRDGH NLISLLEVLS 120
GIKLPREKGR MRFHRLQNVQ IALDFLKQRQ VKLVNIRNDD ITDGNPKLTL GLIWTIILHF 180
QISDIYISGE SGDMSAKEKL LLWTQKVTAG YTGIKCTNFS SCWSDGKMFN ALIHRYRPDL 240
VDMERVQIQS NRENLEQAFE VAERLGVTRL LDAEDVDVPS PDEKSVITYV SSIYDAFPKV 300
PEGGEGISAT EVDSRWQEYQ SRVDSLIPWI KQHTILMSDK TFPQNPVELK ALYNQYIHFK 360
ETEILAKERE KGRIEELYKL LEVWIEFGRI KLPQGYHPND VEEEWGKLII EMLEREKSLR 420
PAVERLELLL QIANKIQNGA LNCEEKLTLA KNTLQADAAH LESGQPVQCE SDVIMYIQEC 480
EGLIRQLQVD LQILRDENYY QLEELAFRVM RLQDELVTLR LECTNLYRKG HFTSLELVPP 540
STLTTTHLKA EPLTKATHSS STSWFRKPMT RAELVAISSS EDEGNLRFVY ELLSWVEEMQ 600
MKLERAEWGN DLPSVELQLE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF HTSYAETLGK 660
LETQYCKLKE TSSFRMRHLQ SLHKFVSRAT AELIWLNEKE EEELAYDWSD NNSNISAKRN 720
YFSELTMELE EKQDVFRSLQ DTAELLSLEN HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ 780
HVKENTAYFQ FFSDARELES FLRNLQDSIK RKYSCDHNTS LSRLEDLLQD SMDEKEQLIQ 840
SKSSVASLVG RSKTIVQLKP RSPDHVLKNT ISVKAVCDYR QIEITICKND ECVLEDNSQR 900
TKWKVISPTG NEAMVPSVCF LIPPPNKDAI EMASRVEQSY QKVMALWHQL HVNTKSLISW 960
NYLRKDLDLV QTWNLEKLRS SAPGECHQIM KNLQAHYEDF LQDSRDSVLF SVADRLRLEE 1020
EVEACKARFQ HLMKSMENED KEETVAKMYI SELKNIRLRL EEYEQRVVKR IQSLASSRTD 1080
RDAWQDNALR IAEQEHTQED LQQLRSDLDA VSMKCDSFLH QSPSSSSVPT LRSELNLLVE 1140
KMDHVYGLST VYLNKLKTVD VIVRSIQDAE LLVKGYEIKL SQEEVVLADL SALEAHWSTL 1200
RHWLSDVKDK NSVFSVLDEE IAKAKVVAEQ MSRLTPERNL DLERYQEKGS QLQERWHRVI 1260
AQLEIRQSEL ESIQEVLGDY RACHGTLIKW IEETTAQQEM MKPGQAEDSR VLSEQLSQQT 1320
ALFAEIERNQ TKLDQCQKFS QQYSTIVKDY ELQLMTYKAF VESQQKSPGK RRRMLSSSDA 1380
ITQEFMDLRT RYTALVTLTT QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKELLGWVST 1440
LARNTQGKAT SSETKESTDI EKAILEQQVL SEELTTKKEQ VSEAIKTSQI FLAKHGHKLS 1500
EKEKKQISEQ LNALNKAYHD LCDGSANQLQ QLQSQLAHQT EQKTLQKQQN TCHQQLEDLC 1560
SWVGQAERAL AGHQGRTTQQ DLSALQKNQS DLKDLQDDIQ NRATSFATVV KDIEGFMEEN 1620
QTKLSPRELT ALREKLHQAK EQYEALQEET RVAQKELEEA VTSALQQETE KSKAAKELAE 1680
NKKKIDALLD WVTSVGSSGG QLLTNLPGME QLSGASLEKG ALDTTDGYMG VNQAPEKLDK 1740
QCEMMKARHQ ELLSQQQNFI LATQSAQAFL DQHGHNLTPE EQQMLQQKLG ELKEQYSTSL 1800
AQSEAELKQV QTLQDELQKF LQDHKEFESW LERSEKELEN MHKGGSSPET LPSLLKRQGS 1860
FSEDVISHKG DLRFVTISGQ KVLDMENSFK EGKEPSEIGN LVKDKLKDAT ERYTALHSKC 1920
TRLGSHLNML LGQYHQFQNS ADSLQAWMQA CEANVEKLLS DTVASDPGVL QEQLATTKQL 1980
QEELAEHQVP VEKLQKVARD IMEIEGEPAP DHRHVQETTD SILSHFQSLS YSLAERSSLL 2040
QKAIAQSQSV QESLESLLQS IGEVEQNLEG KQVSSLSSGV IQEALATNMK LKQDIARQKS 2100
SLEATREMVT RFMETADSTT AAVLQGKLAE VSQRFEQLCL QQQEKESSLK KLLPQAEMFE 2160
HLSGKLQQFM ENKSRMLASG NQPDQDITHF FQQIQELNLE MEDQQENLDT LEHLVTELSS 2220
CGFALDLCQH QDRVQNLRKD FTELQKTVKE REKDASSCQE QLDEFRKLVR TFQKWLKETE 2280
GSIPPTETSM SAKELEKQIE HLKSLLDDWA SKGTLVEEIN CKGTSLENLI MEITAPDSQG 2340
KTGSILPSVG SSVGSVNGYH TCKDLTEIQC DMSDVNLKYE KLGGVLHERQ ESLQAILNRM 2400
EEVHKEANSV LQWLESKEEV LKSMDAMSSP TKTETVKAQA ESNKAFLAEL EQNSPKIQKV 2460
KEALAGLLVT YPNSQEAENW KKIQEELNSR WERATEVTVA RQRQLEESAS HLACFQAAES 2520
QLRPWLMEKE LMMGVLGPLS IDPNMLNAQK QQVQFMLKEF EARRQQHEQL NEAAQGILTG 2580
PGDVSLSTSQ VQKELQSINQ KWVELTDKLN SRSSQIDQAI VKSTQYQELL QDLSEKVRAV 2640
GQRLSVQSAI STQPEAVKQQ LEETSEIRSD LEQLDHEVKE AQTLCDELSV LIGEQYLKDE 2700
LKKRLETVAL PLQGLEDLAA DRINRLQAAL ASTQQFQQMF DELRTWLDDK QSQQAKNCPI 2760
SAKLERLQSQ LQENEEFQKS LNQHSGSYEV IVAEGESLLL SVPPGEEKRT LQNQLVELKN 2820
HWEELSKKTA DRQSRLKDCM QKAQKYQWHV EDLVPWIEDC KAKMSELRVT LDPVQLESSL 2880
LRSKAMLNEV EKRRSLLEIL NSAADILINS SEADEDGIRD EKAGINQNMD AVTEELQAKT 2940
GSLEEMTQRL REFQESFKNI EKKVEGAKHQ LEIFDALGSQ ACSNKNLEKL RAQQEVLQAL 3000
EPQVDYLRNF TQGLVEDAPD GSDASQLLHQ AEVAQQEFLE VKQRVNSGCV MMENKLEGIG 3060
QFHCRVREMF SQLADLDDEL DGMGAIGRDT DSLQSQIEDV RLFLNKIHVL KLDIEASEAE 3120
CRHMLEEEGT LDLLGLKREL EALNKQCGKL TERGKARQEQ LELTLGRVED FYRKLKGLND 3180
ATTAAEEAEA LQWVVGTEVE IINQQLADFK MFQKEQVDPL QMKLQQVNGL GQGLIQSAGK 3240
DCDVQGLEHD MEEINARWNT LNKKVAQRIA QLQEALLHCG KFQDALEPLL SWLADTEELI 3300
ANQKPPSAEY KVVKAQIQEQ KLLQRLLDDR KATVDMLQAE GGRIAQSAEL ADREKITGQL 3360
ESLESRWTEL LSKAAARQKQ LEDILVLAKQ FHETAEPISD FLSVTEKKLA NSEPVGTQTA 3420
KIQQQIIRHK ALEEDIENHA TDVHQAVKIG QSLSSLTSPA EQGVLSEKID SLQARYSEIQ 3480
DRCCRKAALL DQALSNARLF GEDEVEVLNW LAEVEDKLSS VFVKDFKQDV LHRQHADHLA 3540
LNEEIVNRKK NVDQAIKNGQ ALLKQTTGEE VLLIQEKLDG IKTRYADITV TSSKALRTLE 3600
QARQLATKFQ STYEELTGWL REVEEELATS GGQSPTGEQI PQFQQRQKEL KKEVMEHRLV 3660
LDTVNEVSRA LLELVPWRAR EGLDKLVSDA NEQYKLVSDT IGQRVDEIDA AIQRSQQYEQ 3720
AADAELAWVA ETKRKLMALG PIRLEQDQTT AQLQVQKAFS IDIIRHKDSM DELFSHRSEI 3780
FGTCGEEQKT VLQEKTESLI QQYEAISLLN SERYARLERA QVLVNQFWET YEELSPWIEE 3840
TRALIAQLPS PAIDHEQLRQ QQEEMRQLRE SIAEHKPHID KLLKIGPQLK ELNPEEGEMV 3900
EEKYQKAENM YAQIKEEVRQ RALALDEAVS QSTQITEFHD KIEPMLETLE NLSSRLRMPP 3960
LIPAEVDKIR ECISDNKSAT VELEKLQPSF EALKRRGEEL IGRSQGADKD LAAKEIQDKL 4020
DQMVFFWEDI KARAEEREIK FLDVLELAEK FWYDMAALLT TIKDTQDIVH DLESPGIDPS 4080
IIKQQVEAAE TIKEETDGLH EELEFIRILG ADLIFACGET EKPEVRKSID EMNNAWENLN 4140
KTWKERLEKL EDAMQAAVQY QDTLQAMFDW LDNTVIKLCT MPPVGTDLNT VKDQLNEMKE 4200
FKVEVYQQQI EMEKLNHQGE LMLKKATDET DRDIIREPLT ELKHLWENLG EKIAHRQHKL 4260
EGALLALGQF QHALEELMSW LTHTEELLDA QRPISGDPKV IEVELAKHHV LKNDVLAHQA 4320
TVETVNKAGN ELLESSAGDD ASSLRSRLEA MNQCWESVLQ KTEEREQQLQ STLQQAQGFH 4380
SEIEDFLLEL TRMESQLSAS KPTGGLPETA REQLDTHMEL YSQLKAKEET YNQLLDKGRL 4440
MLLSRDDSGS GSKTEQSVAL LEQKWHVVSS KMEERKSKLE EALNLATEFQ NSLQEFINWL 4500
TLAEQSLNIA SPPSLILNTV LSQIEEHKVF ANEVNAHRDQ IIELDQTGNQ LKFLSQKQDV 4560
VLIKNLLVSV QSRWEKVVQR SIERGRSLDD ARKRAKQFHE AWKKLIDWLE DAESHLDSEL 4620
EISNDPDKIK LQLSKHKEFQ KTLGGKQPVY DTTIRTGRAL KEKTLLPEDS QKLDNFLGEV 4680
RDKWDTVCGK SVERQHKLEE ALLFSGQFMD ALQALVDWLY KVEPQLAEDQ PVHGDLDLVM 4740
NLMDAHKVFQ KELGKRTGTV QVLKRSGREL IENSRDDTTW VKGQLQELST RWDTVCKLSV 4800
SKQSRLEQAL KQAEVFRDTV HMLLEWLSEA EQTLRFRGAL PDDTEALQSL IDTHKEFMKK 4860
VEEKRVDVNS AVAMGEVILA VCHPDCITTI KHWITIIRAR FEEVLTWAKQ HQQRLETALS 4920
ELVANAELLE ELLAWIQWAE TTLIQRDQEP IPQNIDRVKA LIAEHQTFME EMTRKQPDVD 4980
RVTKTYKRKN IEPTHAPFIE KSRSGGRKSL SQPTPPPMPI LSQSEAKNPR INQLSARWQQ 5040
VWLLALERQR KLNDALDRLE ELKEFANFDF DVWRKKYMRW MNHKKSRVMD FFRRIDKDQD 5100
GKITRQEFID GILASKFPTT KLEMTAVADI FDRDGDGYID YYEFVAALHP NKDAYRPTTD 5160
ADKIEDEVTR QVAQCKCAKR FQVEQIGENK YRFGDSQQLR LVRILRSTVM VRVGGGWMAL 5220
DEFLVKNDPC RARGRTNIEL REKFILPEGA SQGMTPFRSR GRRSKPSSRA ASPTRSSSSA 5280
SQSNHSCTSM PSSPATPASG TKVIPSSGSK LKRPTPTFHS SRTSLAGDTS NSSSPASTGA 5340
KTNRADPKKS ASRPGSRAGS RAGSRASSRR GSDASDFDLL ETQSACSDTS ESSAAGGQGN 5400
SRRGLNKPSK IPTMSKKTTT ASPRTPGPKR 5430 
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