Full text data of EPPK1
EPPK1
(EPIPL)
[Confidence: low (only semi-automatic identification from reviews)]
Epiplakin (450 kDa epidermal antigen)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Epiplakin (450 kDa epidermal antigen)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P58107
ID EPIPL_HUMAN Reviewed; 5090 AA.
AC P58107; Q76E58;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-JUL-2010, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Epiplakin;
DE AltName: Full=450 kDa epidermal antigen;
GN Name=EPPK1; Synonyms=EPIPL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RX PubMed=11278896; DOI=10.1074/jbc.M011386200;
RA Fujiwara S., Takeo N., Otani Y., Parry D.A.D., Kunimatsu M., Lu R.,
RA Sasaki M., Matsuo N., Khaleduzzaman M., Yoshioka H.;
RT "Epiplakin, a novel member of the plakin family originally identified
RT as a 450-kDa human epidermal autoantigen: structure and tissue
RT localization.";
RL J. Biol. Chem. 276:13340-13347(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14708632; DOI=10.1046/j.1523-1747.2003.12550_5.x;
RA Takeo N., Wang W., Matsuo N., Sumiyoshi H., Yoshioka H., Fujiwara S.;
RT "Structure and heterogeneity of the human gene for epiplakin
RT (EPPK1).";
RL J. Invest. Dermatol. 121:1224-1226(2003).
RN [3]
RP PROTEIN SEQUENCE OF 266-274.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2508; SER-3042;
RP SER-3576; SER-4110 AND SER-4644, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2716; SER-3250;
RP SER-3784; SER-4318 AND SER-4852, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2422; SER-2508;
RP SER-2716; SER-2956; SER-3042; SER-3250; SER-3490; SER-3576; SER-3784;
RP SER-4024; SER-4110; SER-4318; SER-4558; SER-4644 AND SER-4852, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2716; SER-2718;
RP SER-3250; SER-3252; SER-3784; SER-3786; SER-4318; SER-4320; SER-4852
RP AND SER-4854, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver,
CC small intestine, colon, salivary glands, stomach and appendix.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family.
CC -!- SIMILARITY: Contains 65 plectin repeats.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-26 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB40803.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC92750.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB051895; BAB40803.1; ALT_INIT; mRNA.
DR EMBL; AB107036; BAC92750.1; ALT_INIT; Genomic_DNA.
DR UniGene; Hs.743673; -.
DR ProteinModelPortal; P58107; -.
DR SMR; P58107; 43-232, 234-468, 559-798, 882-1165, 1198-1434, 1520-1759, 1849-2087, 2174-2417, 2775-2956, 3309-3490, 3843-4024, 4377-4558, 4911-5085.
DR IntAct; P58107; 8.
DR MINT; MINT-4998630; -.
DR PhosphoSite; P58107; -.
DR DMDM; 300669637; -.
DR PeptideAtlas; P58107; -.
DR PRIDE; P58107; -.
DR UCSC; uc003zaa.1; human.
DR GeneCards; GC08M144935; -.
DR HGNC; HGNC:15577; EPPK1.
DR MIM; 607553; gene.
DR neXtProt; NX_P58107; -.
DR PharmGKB; PA27835; -.
DR HOVERGEN; HBG051491; -.
DR GenomeRNAi; 83481; -.
DR NextBio; 72429; -.
DR PRO; PR:P58107; -.
DR CleanEx; HS_EPPK1; -.
DR Genevestigator; P58107; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR InterPro; IPR001101; Plectin_repeat.
DR Pfam; PF00681; Plectin; 30.
DR SMART; SM00250; PLEC; 65.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 5090 Epiplakin.
FT /FTId=PRO_0000078145.
FT REPEAT 34 71 Plectin 1.
FT REPEAT 72 109 Plectin 2.
FT REPEAT 110 147 Plectin 3.
FT REPEAT 148 185 Plectin 4.
FT REPEAT 192 225 Plectin 5.
FT REPEAT 278 315 Plectin 6.
FT REPEAT 316 353 Plectin 7.
FT REPEAT 355 391 Plectin 8.
FT REPEAT 392 429 Plectin 9.
FT REPEAT 546 583 Plectin 10.
FT REPEAT 603 640 Plectin 11.
FT REPEAT 641 678 Plectin 12.
FT REPEAT 679 716 Plectin 13.
FT REPEAT 717 754 Plectin 14.
FT REPEAT 758 792 Plectin 15.
FT REPEAT 865 903 Plectin 16.
FT REPEAT 923 960 Plectin 17.
FT REPEAT 961 998 Plectin 18.
FT REPEAT 999 1036 Plectin 19.
FT REPEAT 1037 1074 Plectin 20.
FT REPEAT 1239 1276 Plectin 21.
FT REPEAT 1277 1314 Plectin 22.
FT REPEAT 1315 1352 Plectin 23.
FT REPEAT 1353 1390 Plectin 24.
FT REPEAT 1391 1428 Plectin 25.
FT REPEAT 1564 1601 Plectin 26.
FT REPEAT 1602 1639 Plectin 27.
FT REPEAT 1640 1677 Plectin 28.
FT REPEAT 1678 1715 Plectin 29.
FT REPEAT 1719 1753 Plectin 30.
FT REPEAT 1890 1927 Plectin 31.
FT REPEAT 1928 1965 Plectin 32.
FT REPEAT 1966 2003 Plectin 33.
FT REPEAT 2004 2041 Plectin 34.
FT REPEAT 2042 2079 Plectin 35.
FT REPEAT 2217 2259 Plectin 36.
FT REPEAT 2260 2297 Plectin 37.
FT REPEAT 2298 2335 Plectin 38.
FT REPEAT 2336 2373 Plectin 39.
FT REPEAT 2377 2411 Plectin 40.
FT REPEAT 2751 2793 Plectin 41.
FT REPEAT 2794 2831 Plectin 42.
FT REPEAT 2832 2869 Plectin 43.
FT REPEAT 2870 2907 Plectin 44.
FT REPEAT 2911 2945 Plectin 45.
FT REPEAT 3285 3327 Plectin 46.
FT REPEAT 3328 3365 Plectin 47.
FT REPEAT 3366 3403 Plectin 48.
FT REPEAT 3404 3441 Plectin 49.
FT REPEAT 3445 3479 Plectin 50.
FT REPEAT 3819 3861 Plectin 51.
FT REPEAT 3862 3899 Plectin 52.
FT REPEAT 3900 3937 Plectin 53.
FT REPEAT 3938 3975 Plectin 54.
FT REPEAT 3979 4013 Plectin 55.
FT REPEAT 4353 4395 Plectin 56.
FT REPEAT 4396 4433 Plectin 57.
FT REPEAT 4434 4471 Plectin 58.
FT REPEAT 4472 4509 Plectin 59.
FT REPEAT 4513 4547 Plectin 60.
FT REPEAT 4887 4929 Plectin 61.
FT REPEAT 4930 4967 Plectin 62.
FT REPEAT 4968 5005 Plectin 63.
FT REPEAT 5006 5043 Plectin 64.
FT REPEAT 5047 5081 Plectin 65.
FT COILED 1960 1976 Potential.
FT COILED 2618 2649 Potential.
FT COILED 3152 3183 Potential.
FT COILED 3686 3717 Potential.
FT COILED 4220 4251 Potential.
FT COILED 4754 4785 Potential.
FT MOD_RES 1529 1529 Phosphoserine (By similarity).
FT MOD_RES 2422 2422 Phosphoserine.
FT MOD_RES 2508 2508 Phosphoserine.
FT MOD_RES 2716 2716 Phosphoserine.
FT MOD_RES 2718 2718 Phosphoserine.
FT MOD_RES 2956 2956 Phosphoserine.
FT MOD_RES 3042 3042 Phosphoserine.
FT MOD_RES 3250 3250 Phosphoserine.
FT MOD_RES 3252 3252 Phosphoserine.
FT MOD_RES 3490 3490 Phosphoserine.
FT MOD_RES 3576 3576 Phosphoserine.
FT MOD_RES 3784 3784 Phosphoserine.
FT MOD_RES 3786 3786 Phosphoserine.
FT MOD_RES 4024 4024 Phosphoserine.
FT MOD_RES 4110 4110 Phosphoserine.
FT MOD_RES 4318 4318 Phosphoserine.
FT MOD_RES 4320 4320 Phosphoserine.
FT MOD_RES 4558 4558 Phosphoserine.
FT MOD_RES 4644 4644 Phosphoserine.
FT MOD_RES 4852 4852 Phosphoserine.
FT MOD_RES 4854 4854 Phosphoserine.
FT CONFLICT 202 202 N -> D (in Ref. 2; BAC92750).
FT CONFLICT 544 544 E -> K (in Ref. 2; BAC92750).
FT CONFLICT 602 602 A -> V (in Ref. 2; BAC92750).
FT CONFLICT 1618 1618 A -> V (in Ref. 2; BAC92750).
FT CONFLICT 1897 1897 D -> G (in Ref. 2; BAC92750).
FT CONFLICT 2624 2626 Missing (in Ref. 2; BAC92750).
FT CONFLICT 2713 2713 R -> C (in Ref. 2; BAC92750).
FT CONFLICT 2975 2975 T -> M (in Ref. 2; BAC92750).
FT CONFLICT 3162 3162 A -> T (in Ref. 2; BAC92750).
FT CONFLICT 3446 3446 D -> H (in Ref. 2; BAC92750).
FT CONFLICT 3696 3696 A -> T (in Ref. 2; BAC92750).
FT CONFLICT 3841 3841 R -> H (in Ref. 2; BAC92750).
FT CONFLICT 3980 3980 D -> H (in Ref. 2; BAC92750).
FT CONFLICT 4043 4043 T -> M (in Ref. 2; BAC92750).
FT CONFLICT 4080 4080 S -> G (in Ref. 2; BAC92750).
FT CONFLICT 4120 4120 R -> RPS (in Ref. 2; BAC92750).
FT CONFLICT 4149 4149 R -> G (in Ref. 2; BAC92750).
FT CONFLICT 4228 4230 Missing (in Ref. 2; BAC92750).
FT CONFLICT 5068 5068 L -> V (in Ref. 2; BAC92750).
SQ SEQUENCE 5090 AA; 555621 MW; 3A9A74F3C7E167F5 CRC64;
MSGHTLPPLP VPGTNSTEQA SVPRAMAATL GAGTPPRPQA RSIAGVYVEA SGQAQSVYAA
MEQGLLPAGL GQALLEAQAA TGGLVDLARG QLLPVSKALQ QGLVGLELKE KLLAAERATT
GYPDPYGGEK LALFQAIGKE VVDRALGQSW LEVQLATGGL VDPAQGVLVA PEPACHQGLL
DRETWHKLSE LEPGTGDLRF LNPNTLERLT YHQLLERCVR APGSGLALLP LKITFRSMGG
AVSAAELLEV GILDEQAVQG LREGRLAAVD VSARAEVRRY LEGTGSVAGV VLLPEGHKKS
FFQAATEHLL PMGTALPLLE AQAATHTLVD PITGQRLWVD EAVRAGLVSP ELHEQLLVAE
QAVTGHHDPF SGSQIPLFQA MKKGLVDRPL ALRLLDAQLA TGGLVCPARR LRLPLEAALR
CGCLDEDTQR QLSQAGSFSD GTHGGLRYEQ LLALCVTDPE TGLAFLPLSG GPRGGEPQGP
PFIKYSTRQA LSTATATVSV GKFRGRPVSL WELLFSEAIS SEQRAMLAQQ YQEGTLSVEK
LAAELSATLE QAAATARVTF SGLRDTVTPG ELLKAEIIDQ DLYERLEHGQ ATAKDVGSLA
SAQRYLQGTG CIAGLLLPGS QERLSIYEAR CKGLLRPGTA LILLEAQAAT GFIIDPKANK
GHSVEEALRA AVIGPDVFAK LLSAERAVTG YTDPYTGQQI SLFQAMQKGL IVREHGIRLL
EAQIATGGVI DPVHSHRVPV DVAYRRGYFD QMLNLILLDP SDDTKGFFDP NTHENLTYLQ
LLERCVRDPE TGLYLLPLSS TQSPLVDSAT QQAFQNLLLS VKYGRFQGQR VSAWELINSE
YFSEGRRRQL LRRYRQREVT LGQVAKLLEA ETQRQADIML PALRSRVTVH QLLEAGIIDQ
QLLDQVLAGT ISPEALLLMD GVRRYLCGLG AVGGVRLLPS GQRLSLYQAM RQKLLGPRVA
LALLEAQAAT GTIMDPHSPE SLSVDEAVRR GVVGPELYGR LKRAEGAIAG FRDPFSGKQV
SVFQAMKKGL IPWEQAARLL EAQVATGGII DPTSHHHLPM PVAIQRGYVD QEMETALSSS
SETFPTPDGQ GRTSYAQLLE ECPRDETSGL HLLPLPESAP ALPTEEQVQR SLQAVPGAKD
GTSLWDLLSS CHFTEEQRRG LLEDVQEGRT TVPQLLASVQ RWVQETKLLA QARVMVPGPR
GEVPAVWLLD AGIITQETLE ALAQGTQSPA QVAEQPAVKA CLWGTGCVAG VLLQPSGAKA
SIAQAVRDGL LPTGLGQRLL EAQVASGFLV DPLNNQRLSV EDAVKVGLVG RELSEQLGQA
ERAAAGYPDP YSRASLSLWQ AMEKGLVPQN EGLPLLQVQL ATGGVVDPVH GVHLPQAAAC
RLGLLDTQTS QVLTAVDKDN KFFFDPSARD QVTYQQLRER CVCDSETGLL LLPLPSDTVL
EVDDHTAVAL RAMKVPVSTG RFKGCSVSLW DLLLSEYVGA DKRRELVALC RSGRAAALRQ
VVSAVTALVE AAERQPLQAT FRGLRKQVSA RDLFRAQLIS RKTLDELSQG TTTVKEVAEM
DSVKRSLEGG NFIAGVLIQG TQERMSIPEA LRRHILRPGT ALVLLEAQAA TGFIIDPAEN
RKLTVEEAFK AGMFGKETYV KLLSAERAVT GYTDPYTGQQ ISLFQAMQKD LIVREHGIRL
LEAQIATGGI IDPVHSHRVP VDVAYRCGYF DEEMNRILAD PSDDTKGFFD PNTHENLTYL
QLLERCVEDP ETGLYLLQII KKGENYVYIN EATRHVLQSR TAKMRVGRFA DQVVSFWDLL
SSPYFTEDRK RELIQEYGAQ SGGLEKLLEI ITTTIEETET QNQGIKVAAI RGEVTAADLF
NSRVIDQKTL HTLRVGRTGG QALSTLECVK PYLEGSDCIA GVTVPSTREV MSLHEASRKE
LIPAAFATWL LEAQAATGFL LDPCTRQKLS VDEAVDVGLV NEELRERLLK AERAATGYRD
PATGDTIPLF QAMQKQLIEK AEALRLLEVQ VATGGVIDPQ HHHRLPLETA YRRGCLHKDI
YALISDQKHM RKRFVDPNTQ EKVSYRELQE RCRPQEDTGW VLFPVNKAAR DSEHIDDETR
RALEAEQVEI TVGRFRGQKP TLWALLNSEY VTEEKKLQLV RMYRTHTRRA LQTVAQLILE
LIEKQETSNK HLWFQGIRRQ ITASELLSSA IITEEMLQDL ETGRSTTQEL MEDDRVKRYL
EGTSCIAGVL VPAKDQPGRQ EKMSIYQAMW KGVLRPGTAL VLLEAQAATG FVIDPVRNLR
LSVEEPVPAG VVGSEIQEKL LSAERAVTGY TDPYTGQQIS LFQAMQKDLI VREHGIRLLE
AQIATGGVID PVHSHRVPVD VAYRRGYFDE EMNRVLADPS DDTKGFFDPN THENLTYVQL
LRRCVPDPDT GLYMLQLAGR GSAVHQLSEE LRCALRDARV TPGSGALQGQ SVSVWELLFY
REVSEDRRQD LLSRYRAGTL TVEELGATLT SLLAQAQAQA RAEAEAGSPR PDPREALRAA
TMEVKVGRLR GRAVPVWDVL ASGYVSRAAR EELLAEFGSG TLDLPALTRR LTAIIEEAEE
APGARPQLQD ARRGPREPGP AGRGDGDSGR SQREGQGEGE TQEAAAAAAA ARRQEQTLRD
ATMEVQRGQF QGRPVSVWDV LFSSYLSEAR RDELLAQHAA GALGLPDLVA VLTRVIEETE
ERLSKVSFRG LRRQVSASEL HTSGILGPET LRDLAQGTKT LQEVTEMDSV KRYLEGTSCI
AGVLVPAKDQ PGRQEKMSIY QAMWKGVLRP GTALVLLEAQ AATGFVIDPV RNLRLSVEEA
VAAGVVGGEI QEKLLSAERA VTGYTDPYTG QQISLFQAMQ KDLIVREHGI RLLEAQIATG
GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT YVQLLRRCVP
DPDTGLYMLQ LAGRGSAVHQ LSEELRCALR DARVTPGSGA LQGQSVSVWE LLFYREVSED
RRQDLLSRYR AGTLTVEELG ATLTSLLAQA QAQARAEAEA GSPRPDPREA LRAATMEVKV
GRLRGRAVPV WDVLASGYVS GAAREELLAE FGSGTLDLPA LTRRLTAIIE EAEEAPGARP
QLQDAWRGPR EPGPAGRGDG DSGRSQREGQ GEGETQEAAA AAAAARRQEQ TLRDATMEVQ
RGQFQGRPVS VWDVLFSSYL SEARRDELLA QHAAGALGLP DLVAVLTRVI EETEERLSKV
SFRGLRRQVS ASELHTSGIL GPETLRDLAQ GTKTLQEVTE MDSVKRYLEG TSCIAGVLVP
AKDQPGRQEK MSIYQAMWKG VLRPGTALVL LEAQAATGFV IDPVRNLRLS VEEAVAAGVV
GGEIQEKLLS AERAVTGYTD PYTGQQISLF QAMQKDLIVR EHGIRLLEAQ IATGGVIDPV
HSHRVPVDVA YRRGYFDEEM NRVLADPSDD TKGFFDPNTH ENLTYVQLLR RCVPDPDTGL
YMLQLAGRGS AVHQLSEELR CALRDARVTP GSGALQGQSV SVWELLFYRE VSEDRRQDLL
SRYRAGTLTV EELGATLTSL LAQAQAQARA EAEAGSPRPD PREALRAATM EVKVGRLRGR
AVPVWDVLAS GYVSGAAREE LLAEFGSGTL DLPALTRRLT AIIEEAEEAP GARPQLQDAW
RGPREPGPAG RGDGDSGRSQ REGQGEGETQ EAAAAAAAAR RQEQTLRDAT MEVQRGQFQG
RPVSVWDVLF SSYLSEARRD ELLAQHAAGA LGLPDLVAVL TRVIEETEER LSKVSFRGLR
RQVSASELHT SGILGPETLR DLAQGTKTLQ EVTEMDSVKR YLEGTSCIAG VLVPAKDQPG
RQEKMSIYQA MWKGVLRPGT ALVLLEAQAA TGFVIDPVRN LRLSVEEAVA AGVVGGEIQE
KLLSAERAVT GYTDPYTGQQ ISLFQAMQKD LIVREHGIRL LEAQIATGGV IDPVHSHRVP
VDVAYRRGYF DEEMNRVLAD PSDDTKGFFD PNTHENLTYV QLLRRCVPDP DTGLYMLQLA
GRGSAVHQLS EELRCALRDA RVTPGSGALQ GQSVSVWELL FYREVSEDRR QDLLSRYRAS
TLTVEELGAT LTSLLAQAQA QARAEAEAGS PRPDPREALR AATMEVKVGR LRGRAVPVWD
VLASGYVSRA AREELLAEFG SGTLDLPALT RRLTAIIEEA EEAPGARPQL QDAWRGPREP
GPAGRGDGDS GRSQREGQGE GETQEAAAAT AAARRQEQTL RDATMEVQRG QFQGRPVSVW
DVLFSSYLSE ARRDELLAQH AAGALGLPDL VAVLTRVIEE TEERLSKVSF RGLRRQVSAS
ELHTSGILGP ETLRDLAQGT KTLQEVTEMD SVKRYLEGTS CIAGVLVPAK DQPGRQEKMS
IYQAMWKGVL RPGTALVLLE AQAATGFVID PVRNLRLSVE EAVAAGVVGG EIQEKLLSAE
RAVTGYTDPY TGQQISLFQA MQKDLIVREH GIRLLEAQIA TGGVIDPVHS HRVPVDVAYR
RGYFDEEMNR VLADPSDDTK GFFDPNTHEN LTYVQLLRRC VPDPDTGLYM LQLAGRGSAV
HQLSEELRCA LRDARVTPGS GALQGQSVSV WELLFYREVS EDRRQDLLSR YRAGTLTVEE
LGATLTSLLA QAQAQARAEA EAGSPRPDPR EALRAATMEV KVGRLRGRAV PVWDVLASGY
VSGAAREELL AEFGSGTLDL PALTRRLTAI IEEAEEAPGA RPQLQDAWRG PREPGPAGRG
DGDSGRSQRE GQGEGETQEA AAAAAAARRQ EQTLRDATME VQRGQFQGRP VSVWDVLFSS
YLSEARRDEL LAQHAAGALG LPDLVAVLTR VIEETEERLS KVSFRGLRRQ VSASELHTSG
ILGPETLRDL AQGTKTLQEV TEMDSVKRYL EGTSCIAGVL VPAKDQPGRQ EKMSIYQAMW
KGVLRPGTAL VLLEAQAATG FVIDPVRNLR LSVEEAVAAG VVGGEIQEKL LSAERAVTGY
TDPYTGQQIS LFQAMQKDLI VREHGIRLLE AQIATGGVID PVHSHRVPVD VAYRRGYFDE
EMNRVLADPS DDTKGFFDPN THENLTYLQL LQRATLDPET GLLFLSLSLQ
//
ID EPIPL_HUMAN Reviewed; 5090 AA.
AC P58107; Q76E58;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-JUL-2010, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Epiplakin;
DE AltName: Full=450 kDa epidermal antigen;
GN Name=EPPK1; Synonyms=EPIPL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervix carcinoma;
RX PubMed=11278896; DOI=10.1074/jbc.M011386200;
RA Fujiwara S., Takeo N., Otani Y., Parry D.A.D., Kunimatsu M., Lu R.,
RA Sasaki M., Matsuo N., Khaleduzzaman M., Yoshioka H.;
RT "Epiplakin, a novel member of the plakin family originally identified
RT as a 450-kDa human epidermal autoantigen: structure and tissue
RT localization.";
RL J. Biol. Chem. 276:13340-13347(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14708632; DOI=10.1046/j.1523-1747.2003.12550_5.x;
RA Takeo N., Wang W., Matsuo N., Sumiyoshi H., Yoshioka H., Fujiwara S.;
RT "Structure and heterogeneity of the human gene for epiplakin
RT (EPPK1).";
RL J. Invest. Dermatol. 121:1224-1226(2003).
RN [3]
RP PROTEIN SEQUENCE OF 266-274.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2508; SER-3042;
RP SER-3576; SER-4110 AND SER-4644, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2716; SER-3250;
RP SER-3784; SER-4318 AND SER-4852, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2422; SER-2508;
RP SER-2716; SER-2956; SER-3042; SER-3250; SER-3490; SER-3576; SER-3784;
RP SER-4024; SER-4110; SER-4318; SER-4558; SER-4644 AND SER-4852, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2716; SER-2718;
RP SER-3250; SER-3252; SER-3784; SER-3786; SER-4318; SER-4320; SER-4852
RP AND SER-4854, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver,
CC small intestine, colon, salivary glands, stomach and appendix.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family.
CC -!- SIMILARITY: Contains 65 plectin repeats.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-26 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB40803.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAC92750.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AB051895; BAB40803.1; ALT_INIT; mRNA.
DR EMBL; AB107036; BAC92750.1; ALT_INIT; Genomic_DNA.
DR UniGene; Hs.743673; -.
DR ProteinModelPortal; P58107; -.
DR SMR; P58107; 43-232, 234-468, 559-798, 882-1165, 1198-1434, 1520-1759, 1849-2087, 2174-2417, 2775-2956, 3309-3490, 3843-4024, 4377-4558, 4911-5085.
DR IntAct; P58107; 8.
DR MINT; MINT-4998630; -.
DR PhosphoSite; P58107; -.
DR DMDM; 300669637; -.
DR PeptideAtlas; P58107; -.
DR PRIDE; P58107; -.
DR UCSC; uc003zaa.1; human.
DR GeneCards; GC08M144935; -.
DR HGNC; HGNC:15577; EPPK1.
DR MIM; 607553; gene.
DR neXtProt; NX_P58107; -.
DR PharmGKB; PA27835; -.
DR HOVERGEN; HBG051491; -.
DR GenomeRNAi; 83481; -.
DR NextBio; 72429; -.
DR PRO; PR:P58107; -.
DR CleanEx; HS_EPPK1; -.
DR Genevestigator; P58107; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR InterPro; IPR001101; Plectin_repeat.
DR Pfam; PF00681; Plectin; 30.
DR SMART; SM00250; PLEC; 65.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 5090 Epiplakin.
FT /FTId=PRO_0000078145.
FT REPEAT 34 71 Plectin 1.
FT REPEAT 72 109 Plectin 2.
FT REPEAT 110 147 Plectin 3.
FT REPEAT 148 185 Plectin 4.
FT REPEAT 192 225 Plectin 5.
FT REPEAT 278 315 Plectin 6.
FT REPEAT 316 353 Plectin 7.
FT REPEAT 355 391 Plectin 8.
FT REPEAT 392 429 Plectin 9.
FT REPEAT 546 583 Plectin 10.
FT REPEAT 603 640 Plectin 11.
FT REPEAT 641 678 Plectin 12.
FT REPEAT 679 716 Plectin 13.
FT REPEAT 717 754 Plectin 14.
FT REPEAT 758 792 Plectin 15.
FT REPEAT 865 903 Plectin 16.
FT REPEAT 923 960 Plectin 17.
FT REPEAT 961 998 Plectin 18.
FT REPEAT 999 1036 Plectin 19.
FT REPEAT 1037 1074 Plectin 20.
FT REPEAT 1239 1276 Plectin 21.
FT REPEAT 1277 1314 Plectin 22.
FT REPEAT 1315 1352 Plectin 23.
FT REPEAT 1353 1390 Plectin 24.
FT REPEAT 1391 1428 Plectin 25.
FT REPEAT 1564 1601 Plectin 26.
FT REPEAT 1602 1639 Plectin 27.
FT REPEAT 1640 1677 Plectin 28.
FT REPEAT 1678 1715 Plectin 29.
FT REPEAT 1719 1753 Plectin 30.
FT REPEAT 1890 1927 Plectin 31.
FT REPEAT 1928 1965 Plectin 32.
FT REPEAT 1966 2003 Plectin 33.
FT REPEAT 2004 2041 Plectin 34.
FT REPEAT 2042 2079 Plectin 35.
FT REPEAT 2217 2259 Plectin 36.
FT REPEAT 2260 2297 Plectin 37.
FT REPEAT 2298 2335 Plectin 38.
FT REPEAT 2336 2373 Plectin 39.
FT REPEAT 2377 2411 Plectin 40.
FT REPEAT 2751 2793 Plectin 41.
FT REPEAT 2794 2831 Plectin 42.
FT REPEAT 2832 2869 Plectin 43.
FT REPEAT 2870 2907 Plectin 44.
FT REPEAT 2911 2945 Plectin 45.
FT REPEAT 3285 3327 Plectin 46.
FT REPEAT 3328 3365 Plectin 47.
FT REPEAT 3366 3403 Plectin 48.
FT REPEAT 3404 3441 Plectin 49.
FT REPEAT 3445 3479 Plectin 50.
FT REPEAT 3819 3861 Plectin 51.
FT REPEAT 3862 3899 Plectin 52.
FT REPEAT 3900 3937 Plectin 53.
FT REPEAT 3938 3975 Plectin 54.
FT REPEAT 3979 4013 Plectin 55.
FT REPEAT 4353 4395 Plectin 56.
FT REPEAT 4396 4433 Plectin 57.
FT REPEAT 4434 4471 Plectin 58.
FT REPEAT 4472 4509 Plectin 59.
FT REPEAT 4513 4547 Plectin 60.
FT REPEAT 4887 4929 Plectin 61.
FT REPEAT 4930 4967 Plectin 62.
FT REPEAT 4968 5005 Plectin 63.
FT REPEAT 5006 5043 Plectin 64.
FT REPEAT 5047 5081 Plectin 65.
FT COILED 1960 1976 Potential.
FT COILED 2618 2649 Potential.
FT COILED 3152 3183 Potential.
FT COILED 3686 3717 Potential.
FT COILED 4220 4251 Potential.
FT COILED 4754 4785 Potential.
FT MOD_RES 1529 1529 Phosphoserine (By similarity).
FT MOD_RES 2422 2422 Phosphoserine.
FT MOD_RES 2508 2508 Phosphoserine.
FT MOD_RES 2716 2716 Phosphoserine.
FT MOD_RES 2718 2718 Phosphoserine.
FT MOD_RES 2956 2956 Phosphoserine.
FT MOD_RES 3042 3042 Phosphoserine.
FT MOD_RES 3250 3250 Phosphoserine.
FT MOD_RES 3252 3252 Phosphoserine.
FT MOD_RES 3490 3490 Phosphoserine.
FT MOD_RES 3576 3576 Phosphoserine.
FT MOD_RES 3784 3784 Phosphoserine.
FT MOD_RES 3786 3786 Phosphoserine.
FT MOD_RES 4024 4024 Phosphoserine.
FT MOD_RES 4110 4110 Phosphoserine.
FT MOD_RES 4318 4318 Phosphoserine.
FT MOD_RES 4320 4320 Phosphoserine.
FT MOD_RES 4558 4558 Phosphoserine.
FT MOD_RES 4644 4644 Phosphoserine.
FT MOD_RES 4852 4852 Phosphoserine.
FT MOD_RES 4854 4854 Phosphoserine.
FT CONFLICT 202 202 N -> D (in Ref. 2; BAC92750).
FT CONFLICT 544 544 E -> K (in Ref. 2; BAC92750).
FT CONFLICT 602 602 A -> V (in Ref. 2; BAC92750).
FT CONFLICT 1618 1618 A -> V (in Ref. 2; BAC92750).
FT CONFLICT 1897 1897 D -> G (in Ref. 2; BAC92750).
FT CONFLICT 2624 2626 Missing (in Ref. 2; BAC92750).
FT CONFLICT 2713 2713 R -> C (in Ref. 2; BAC92750).
FT CONFLICT 2975 2975 T -> M (in Ref. 2; BAC92750).
FT CONFLICT 3162 3162 A -> T (in Ref. 2; BAC92750).
FT CONFLICT 3446 3446 D -> H (in Ref. 2; BAC92750).
FT CONFLICT 3696 3696 A -> T (in Ref. 2; BAC92750).
FT CONFLICT 3841 3841 R -> H (in Ref. 2; BAC92750).
FT CONFLICT 3980 3980 D -> H (in Ref. 2; BAC92750).
FT CONFLICT 4043 4043 T -> M (in Ref. 2; BAC92750).
FT CONFLICT 4080 4080 S -> G (in Ref. 2; BAC92750).
FT CONFLICT 4120 4120 R -> RPS (in Ref. 2; BAC92750).
FT CONFLICT 4149 4149 R -> G (in Ref. 2; BAC92750).
FT CONFLICT 4228 4230 Missing (in Ref. 2; BAC92750).
FT CONFLICT 5068 5068 L -> V (in Ref. 2; BAC92750).
SQ SEQUENCE 5090 AA; 555621 MW; 3A9A74F3C7E167F5 CRC64;
MSGHTLPPLP VPGTNSTEQA SVPRAMAATL GAGTPPRPQA RSIAGVYVEA SGQAQSVYAA
MEQGLLPAGL GQALLEAQAA TGGLVDLARG QLLPVSKALQ QGLVGLELKE KLLAAERATT
GYPDPYGGEK LALFQAIGKE VVDRALGQSW LEVQLATGGL VDPAQGVLVA PEPACHQGLL
DRETWHKLSE LEPGTGDLRF LNPNTLERLT YHQLLERCVR APGSGLALLP LKITFRSMGG
AVSAAELLEV GILDEQAVQG LREGRLAAVD VSARAEVRRY LEGTGSVAGV VLLPEGHKKS
FFQAATEHLL PMGTALPLLE AQAATHTLVD PITGQRLWVD EAVRAGLVSP ELHEQLLVAE
QAVTGHHDPF SGSQIPLFQA MKKGLVDRPL ALRLLDAQLA TGGLVCPARR LRLPLEAALR
CGCLDEDTQR QLSQAGSFSD GTHGGLRYEQ LLALCVTDPE TGLAFLPLSG GPRGGEPQGP
PFIKYSTRQA LSTATATVSV GKFRGRPVSL WELLFSEAIS SEQRAMLAQQ YQEGTLSVEK
LAAELSATLE QAAATARVTF SGLRDTVTPG ELLKAEIIDQ DLYERLEHGQ ATAKDVGSLA
SAQRYLQGTG CIAGLLLPGS QERLSIYEAR CKGLLRPGTA LILLEAQAAT GFIIDPKANK
GHSVEEALRA AVIGPDVFAK LLSAERAVTG YTDPYTGQQI SLFQAMQKGL IVREHGIRLL
EAQIATGGVI DPVHSHRVPV DVAYRRGYFD QMLNLILLDP SDDTKGFFDP NTHENLTYLQ
LLERCVRDPE TGLYLLPLSS TQSPLVDSAT QQAFQNLLLS VKYGRFQGQR VSAWELINSE
YFSEGRRRQL LRRYRQREVT LGQVAKLLEA ETQRQADIML PALRSRVTVH QLLEAGIIDQ
QLLDQVLAGT ISPEALLLMD GVRRYLCGLG AVGGVRLLPS GQRLSLYQAM RQKLLGPRVA
LALLEAQAAT GTIMDPHSPE SLSVDEAVRR GVVGPELYGR LKRAEGAIAG FRDPFSGKQV
SVFQAMKKGL IPWEQAARLL EAQVATGGII DPTSHHHLPM PVAIQRGYVD QEMETALSSS
SETFPTPDGQ GRTSYAQLLE ECPRDETSGL HLLPLPESAP ALPTEEQVQR SLQAVPGAKD
GTSLWDLLSS CHFTEEQRRG LLEDVQEGRT TVPQLLASVQ RWVQETKLLA QARVMVPGPR
GEVPAVWLLD AGIITQETLE ALAQGTQSPA QVAEQPAVKA CLWGTGCVAG VLLQPSGAKA
SIAQAVRDGL LPTGLGQRLL EAQVASGFLV DPLNNQRLSV EDAVKVGLVG RELSEQLGQA
ERAAAGYPDP YSRASLSLWQ AMEKGLVPQN EGLPLLQVQL ATGGVVDPVH GVHLPQAAAC
RLGLLDTQTS QVLTAVDKDN KFFFDPSARD QVTYQQLRER CVCDSETGLL LLPLPSDTVL
EVDDHTAVAL RAMKVPVSTG RFKGCSVSLW DLLLSEYVGA DKRRELVALC RSGRAAALRQ
VVSAVTALVE AAERQPLQAT FRGLRKQVSA RDLFRAQLIS RKTLDELSQG TTTVKEVAEM
DSVKRSLEGG NFIAGVLIQG TQERMSIPEA LRRHILRPGT ALVLLEAQAA TGFIIDPAEN
RKLTVEEAFK AGMFGKETYV KLLSAERAVT GYTDPYTGQQ ISLFQAMQKD LIVREHGIRL
LEAQIATGGI IDPVHSHRVP VDVAYRCGYF DEEMNRILAD PSDDTKGFFD PNTHENLTYL
QLLERCVEDP ETGLYLLQII KKGENYVYIN EATRHVLQSR TAKMRVGRFA DQVVSFWDLL
SSPYFTEDRK RELIQEYGAQ SGGLEKLLEI ITTTIEETET QNQGIKVAAI RGEVTAADLF
NSRVIDQKTL HTLRVGRTGG QALSTLECVK PYLEGSDCIA GVTVPSTREV MSLHEASRKE
LIPAAFATWL LEAQAATGFL LDPCTRQKLS VDEAVDVGLV NEELRERLLK AERAATGYRD
PATGDTIPLF QAMQKQLIEK AEALRLLEVQ VATGGVIDPQ HHHRLPLETA YRRGCLHKDI
YALISDQKHM RKRFVDPNTQ EKVSYRELQE RCRPQEDTGW VLFPVNKAAR DSEHIDDETR
RALEAEQVEI TVGRFRGQKP TLWALLNSEY VTEEKKLQLV RMYRTHTRRA LQTVAQLILE
LIEKQETSNK HLWFQGIRRQ ITASELLSSA IITEEMLQDL ETGRSTTQEL MEDDRVKRYL
EGTSCIAGVL VPAKDQPGRQ EKMSIYQAMW KGVLRPGTAL VLLEAQAATG FVIDPVRNLR
LSVEEPVPAG VVGSEIQEKL LSAERAVTGY TDPYTGQQIS LFQAMQKDLI VREHGIRLLE
AQIATGGVID PVHSHRVPVD VAYRRGYFDE EMNRVLADPS DDTKGFFDPN THENLTYVQL
LRRCVPDPDT GLYMLQLAGR GSAVHQLSEE LRCALRDARV TPGSGALQGQ SVSVWELLFY
REVSEDRRQD LLSRYRAGTL TVEELGATLT SLLAQAQAQA RAEAEAGSPR PDPREALRAA
TMEVKVGRLR GRAVPVWDVL ASGYVSRAAR EELLAEFGSG TLDLPALTRR LTAIIEEAEE
APGARPQLQD ARRGPREPGP AGRGDGDSGR SQREGQGEGE TQEAAAAAAA ARRQEQTLRD
ATMEVQRGQF QGRPVSVWDV LFSSYLSEAR RDELLAQHAA GALGLPDLVA VLTRVIEETE
ERLSKVSFRG LRRQVSASEL HTSGILGPET LRDLAQGTKT LQEVTEMDSV KRYLEGTSCI
AGVLVPAKDQ PGRQEKMSIY QAMWKGVLRP GTALVLLEAQ AATGFVIDPV RNLRLSVEEA
VAAGVVGGEI QEKLLSAERA VTGYTDPYTG QQISLFQAMQ KDLIVREHGI RLLEAQIATG
GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT YVQLLRRCVP
DPDTGLYMLQ LAGRGSAVHQ LSEELRCALR DARVTPGSGA LQGQSVSVWE LLFYREVSED
RRQDLLSRYR AGTLTVEELG ATLTSLLAQA QAQARAEAEA GSPRPDPREA LRAATMEVKV
GRLRGRAVPV WDVLASGYVS GAAREELLAE FGSGTLDLPA LTRRLTAIIE EAEEAPGARP
QLQDAWRGPR EPGPAGRGDG DSGRSQREGQ GEGETQEAAA AAAAARRQEQ TLRDATMEVQ
RGQFQGRPVS VWDVLFSSYL SEARRDELLA QHAAGALGLP DLVAVLTRVI EETEERLSKV
SFRGLRRQVS ASELHTSGIL GPETLRDLAQ GTKTLQEVTE MDSVKRYLEG TSCIAGVLVP
AKDQPGRQEK MSIYQAMWKG VLRPGTALVL LEAQAATGFV IDPVRNLRLS VEEAVAAGVV
GGEIQEKLLS AERAVTGYTD PYTGQQISLF QAMQKDLIVR EHGIRLLEAQ IATGGVIDPV
HSHRVPVDVA YRRGYFDEEM NRVLADPSDD TKGFFDPNTH ENLTYVQLLR RCVPDPDTGL
YMLQLAGRGS AVHQLSEELR CALRDARVTP GSGALQGQSV SVWELLFYRE VSEDRRQDLL
SRYRAGTLTV EELGATLTSL LAQAQAQARA EAEAGSPRPD PREALRAATM EVKVGRLRGR
AVPVWDVLAS GYVSGAAREE LLAEFGSGTL DLPALTRRLT AIIEEAEEAP GARPQLQDAW
RGPREPGPAG RGDGDSGRSQ REGQGEGETQ EAAAAAAAAR RQEQTLRDAT MEVQRGQFQG
RPVSVWDVLF SSYLSEARRD ELLAQHAAGA LGLPDLVAVL TRVIEETEER LSKVSFRGLR
RQVSASELHT SGILGPETLR DLAQGTKTLQ EVTEMDSVKR YLEGTSCIAG VLVPAKDQPG
RQEKMSIYQA MWKGVLRPGT ALVLLEAQAA TGFVIDPVRN LRLSVEEAVA AGVVGGEIQE
KLLSAERAVT GYTDPYTGQQ ISLFQAMQKD LIVREHGIRL LEAQIATGGV IDPVHSHRVP
VDVAYRRGYF DEEMNRVLAD PSDDTKGFFD PNTHENLTYV QLLRRCVPDP DTGLYMLQLA
GRGSAVHQLS EELRCALRDA RVTPGSGALQ GQSVSVWELL FYREVSEDRR QDLLSRYRAS
TLTVEELGAT LTSLLAQAQA QARAEAEAGS PRPDPREALR AATMEVKVGR LRGRAVPVWD
VLASGYVSRA AREELLAEFG SGTLDLPALT RRLTAIIEEA EEAPGARPQL QDAWRGPREP
GPAGRGDGDS GRSQREGQGE GETQEAAAAT AAARRQEQTL RDATMEVQRG QFQGRPVSVW
DVLFSSYLSE ARRDELLAQH AAGALGLPDL VAVLTRVIEE TEERLSKVSF RGLRRQVSAS
ELHTSGILGP ETLRDLAQGT KTLQEVTEMD SVKRYLEGTS CIAGVLVPAK DQPGRQEKMS
IYQAMWKGVL RPGTALVLLE AQAATGFVID PVRNLRLSVE EAVAAGVVGG EIQEKLLSAE
RAVTGYTDPY TGQQISLFQA MQKDLIVREH GIRLLEAQIA TGGVIDPVHS HRVPVDVAYR
RGYFDEEMNR VLADPSDDTK GFFDPNTHEN LTYVQLLRRC VPDPDTGLYM LQLAGRGSAV
HQLSEELRCA LRDARVTPGS GALQGQSVSV WELLFYREVS EDRRQDLLSR YRAGTLTVEE
LGATLTSLLA QAQAQARAEA EAGSPRPDPR EALRAATMEV KVGRLRGRAV PVWDVLASGY
VSGAAREELL AEFGSGTLDL PALTRRLTAI IEEAEEAPGA RPQLQDAWRG PREPGPAGRG
DGDSGRSQRE GQGEGETQEA AAAAAAARRQ EQTLRDATME VQRGQFQGRP VSVWDVLFSS
YLSEARRDEL LAQHAAGALG LPDLVAVLTR VIEETEERLS KVSFRGLRRQ VSASELHTSG
ILGPETLRDL AQGTKTLQEV TEMDSVKRYL EGTSCIAGVL VPAKDQPGRQ EKMSIYQAMW
KGVLRPGTAL VLLEAQAATG FVIDPVRNLR LSVEEAVAAG VVGGEIQEKL LSAERAVTGY
TDPYTGQQIS LFQAMQKDLI VREHGIRLLE AQIATGGVID PVHSHRVPVD VAYRRGYFDE
EMNRVLADPS DDTKGFFDPN THENLTYLQL LQRATLDPET GLLFLSLSLQ
//
MIM
607553
*RECORD*
*FIELD* NO
607553
*FIELD* TI
*607553 EPIPLAKIN 1; EPPK1
*FIELD* TX
CLONING
Fujiwara et al. (2001) described a patient with a subepidermal
read moreblistering disease that resembled bullous pemphigoid both clinically and
pathologically. Using the patient serum, they obtained a cDNA clone for
the antigenic protein, which they called epiplakin, from a human
keratinocyte expression library. They obtained full-length EPPK1 cDNA
from HeLa cell and genomic cDNA libraries. The deduced protein contains
5,065 amino acids and has a calculated molecular mass of more than 552
kD. Epiplakin has 13 domains that are homologous to the C-terminal B
domain of desmoplakin (125647). B domains 9 through 13 and their
preceding 358-residue linker regions form 5 repeats that share almost
100% identity and contain a 7-residue epitope recognized by the patient
serum. Unlike desmoplakin, epiplakin lacks a coiled-coil rod domain, an
N-terminal domain, and a dimerization motif, which suggests that it
exists as a single-chain structure. Northern dot blot analysis detected
expression in a wide variety of tissues. Highest expression was in
liver, small intestine, colon, salivary glands, stomach, and appendix,
with lower expression in placenta, lung, brain, and bone marrow.
Immunofluorescence staining of human skin detected epiplakin in the
entire epidermis, with prominent staining of basal keratinocytes.
Staining was found in all layers of the stratified epithelium of
esophagus, in acinous cells of the parotid gland, and in mucous
epithelial cells of the stomach and colon.
*FIELD* RF
1. Fujiwara, S.; Takeo, N.; Otani, Y.; Parry, D. A. D.; Kunimatsu,
M.; Lu, R.; Sasaki, M.; Matsuo, N.; Khaleduzzaman, M.; Yoshioka, H.
: Epiplakin, a novel member of the plakin family originally identified
as a 450-kDa human epidermal autoantigen: structure and tissue localization. J.
Biol. Chem. 276: 13340-13347, 2001.
*FIELD* CD
Patricia A. Hartz: 2/6/2003
*FIELD* ED
mgross: 02/06/2003
*RECORD*
*FIELD* NO
607553
*FIELD* TI
*607553 EPIPLAKIN 1; EPPK1
*FIELD* TX
CLONING
Fujiwara et al. (2001) described a patient with a subepidermal
read moreblistering disease that resembled bullous pemphigoid both clinically and
pathologically. Using the patient serum, they obtained a cDNA clone for
the antigenic protein, which they called epiplakin, from a human
keratinocyte expression library. They obtained full-length EPPK1 cDNA
from HeLa cell and genomic cDNA libraries. The deduced protein contains
5,065 amino acids and has a calculated molecular mass of more than 552
kD. Epiplakin has 13 domains that are homologous to the C-terminal B
domain of desmoplakin (125647). B domains 9 through 13 and their
preceding 358-residue linker regions form 5 repeats that share almost
100% identity and contain a 7-residue epitope recognized by the patient
serum. Unlike desmoplakin, epiplakin lacks a coiled-coil rod domain, an
N-terminal domain, and a dimerization motif, which suggests that it
exists as a single-chain structure. Northern dot blot analysis detected
expression in a wide variety of tissues. Highest expression was in
liver, small intestine, colon, salivary glands, stomach, and appendix,
with lower expression in placenta, lung, brain, and bone marrow.
Immunofluorescence staining of human skin detected epiplakin in the
entire epidermis, with prominent staining of basal keratinocytes.
Staining was found in all layers of the stratified epithelium of
esophagus, in acinous cells of the parotid gland, and in mucous
epithelial cells of the stomach and colon.
*FIELD* RF
1. Fujiwara, S.; Takeo, N.; Otani, Y.; Parry, D. A. D.; Kunimatsu,
M.; Lu, R.; Sasaki, M.; Matsuo, N.; Khaleduzzaman, M.; Yoshioka, H.
: Epiplakin, a novel member of the plakin family originally identified
as a 450-kDa human epidermal autoantigen: structure and tissue localization. J.
Biol. Chem. 276: 13340-13347, 2001.
*FIELD* CD
Patricia A. Hartz: 2/6/2003
*FIELD* ED
mgross: 02/06/2003