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Reviewed, UniProtKB/Swiss-Prot Q15149 (PLEC1_HUMAN)

Last modified February 9, 2010. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Plectin-1
      Short name=PLTN
      Short name=PCN
Alternative name(s):
    Hemidesmosomal protein 1
      Short name=HD1
Gene names
Name: PLEC1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length4684 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the cross-linking and stabilization of cytoskeletal intermediate filaments network, but also in the regulation of their dynamics.

Subunit structure

Homodimer or homotetramer. Interacts with Nesprin-3 By similarity.

Subcellular location

Cytoplasm › cytoskeleton.

Tissue specificity

Widely expressed with highest levels in muscle, heart, placenta and spinal cord.

Domain

The N-terminus interacts with actin, the C-terminus with vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N- and the C-terminus can bind integrin beta-4.

Post-translational modification

Phosphorylated by CDC2; regulates dissociation from intermediate filaments during mitosis By similarity. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24

Involvement in disease

Defects in PLEC1 are the cause of epidermolysis bullosa simplex with pyloric atresia (EBS-PA) [MIM:612138]. EBS-PA is an autosomal recessive genodermatosis characterized by severe skin blistering at birth and congenital pyloric atresia. Death usually occurs in infancy. This disorder is allelic to MD-EBS. Ref.2 Ref.31

Defects in PLEC1 are the cause of epidermolysis bullosa simplex with muscular dystrophy (MD-EBS) [MIM:226670]. MD-EBS is an autosomal recessive disorder characterized by epidermal blister formation at the level of the hemidesmosome and associated with late-onset muscular dystrophy.

Defects in PLEC1 are the cause of epidermolysis bullosa simplex Ogna type (O-EBS) [MIM:131950]; also called epidermolysis bullosa simplex 1. O-EBS is a form of intraepidermal epidermolysis bullosa characterized by generalized skin bruising, skin fragility with non-scarring blistering and small hemorrhagic blisters on hands. At the ultrastructural level, it is differentiated from classical cases of K-EBS, WC-EBS and DM-EBS, by the occurrence of blisters originating in basal cells above hemidesmosomes, and abnormal hemidesmosome intracellular attachment plates.

Sequence similarities

Belongs to the plakin or cytolinker family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 33 plectin repeats.

Contains 4 spectrin repeats.

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Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Epidermolysis bullosa
   DomainCoiled coil
Repeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processhemidesmosome assembly

Inferred from Experiment. Source: Reactome

   Cellular componentcytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from Experiment. Source: Reactome

plasma membrane Ref.1

Non-traceable author statement. Source: ProtInc

   Molecular functionactin binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of muscle

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15149-1)

Also known as: Plectin-6;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15149-2)

Also known as: Plectin-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA
Isoform 3 (identifier: Q15149-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSGEDAEVRA...PAERAVIRIA
     409-412: Missing.
Isoform 4 (identifier: Q15149-4)

Also known as: Plectin-11;

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MVAGMLMPRD...RPGPEPAPAT → MSQHQLRVPQ...AVLRASEGKK
Note: Phosphorylated on Ser-21 and Tyr-26.
Isoform 5 (identifier: Q15149-5)

Also known as: Plectin-8;

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
     138-174: RVYRRKELEEVSPETPVVPATTQRTLARPGPEPAPAT → MEPSGSLFPSLVVVGHVVTLAAVWHWRRGRRWAQDEQ
Isoform 6 (identifier: Q15149-6)

Also known as: Plectin-10;

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     134-174: TEEQRVYRRK...RPGPEPAPAT → MSGAGGAFAS...GYLYQQLCCV
Isoform 7 (identifier: Q15149-7)

Also known as: Plectin-7;

The sequence of this isoform differs from the canonical sequence as follows:
     1-169: Missing.
     170-174: PAPAT → MKIVP
Isoform 8 (identifier: Q15149-8)

Also known as: Plectin-3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: Missing.
     160-174: QRTLARPGPEPAPAT → MDPSRAIQNEISSLK
Isoform 9 (identifier: Q15149-9)

Also known as: Plectin-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     152-174: TPVVPATTQRTLARPGPEPAPAT → MAGPLPDEQDFIQAYEEVREKYK

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 46844684Plectin-1
PRO_0000078135

Regions

Domain175 – 400226Actin-binding
Domain179 – 282104CH 1
Domain295 – 397103CH 2
Repeat645 – 71066Spectrin 1
Repeat740 – 82485Spectrin 2
Repeat837 – 93094Spectrin 3
Repeat1315 – 1415101Spectrin 4
Repeat2826 – 286338Plectin 1
Repeat2864 – 290138Plectin 2
Repeat2902 – 293938Plectin 3
Repeat2940 – 297738Plectin 4
Repeat2981 – 301535Plectin 5
Repeat3116 – 315338Plectin 6
Repeat3154 – 319138Plectin 7
Repeat3192 – 322938Plectin 8
Repeat3230 – 326738Plectin 9
Repeat3268 – 330538Plectin 10
Repeat3306 – 334338Plectin 11
Repeat3485 – 352238Plectin 12
Repeat3523 – 356038Plectin 13
Repeat3561 – 359838Plectin 14
Repeat3599 – 363638Plectin 15
Repeat3640 – 367435Plectin 16
Repeat3820 – 385738Plectin 17
Repeat3858 – 389538Plectin 18
Repeat3896 – 393338Plectin 19
Repeat3934 – 397138Plectin 20
Repeat3975 – 400834Plectin 21
Repeat4063 – 410038Plectin 22
Repeat4101 – 413838Plectin 23
Repeat4139 – 417638Plectin 24
Repeat4177 – 421438Plectin 25
Repeat4218 – 425235Plectin 26
Repeat4265 – 430541Plectin 27
Repeat4319 – 435638Plectin 28
Repeat4408 – 444538Plectin 29
Repeat4446 – 448338Plectin 30
Repeat4484 – 452138Plectin 31
Repeat4522 – 455938Plectin 32
Repeat4560 – 459738Plectin 33
Region1 – 14701470Globular 1
Region1471 – 27551285Central fibrous rod domain
Region2756 – 46841929Globular 2
Region4250 – 430051Binding to intermediate filaments By similarity
Region4625 – 4640164 X 4 AA tandem repeats of G-S-R-X
Coiled coil1469 – 27561288 Potential

Amino acid modifications

Modified residue1251Phosphoserine Ref.11 Ref.18 Ref.19
Modified residue1491Phosphoserine Ref.11 Ref.16 Ref.19
Modified residue1871N6-acetyllysine Ref.25
Modified residue2011Phosphoserine By similarity
Modified residue7201Phosphoserine Ref.6 Ref.11 Ref.16 Ref.18 Ref.19
Modified residue7821Phosphoserine Ref.10
Modified residue14351Phosphoserine Ref.6 Ref.11 Ref.12 Ref.14 Ref.16 Ref.18 Ref.19 Ref.21
Modified residue14441Phosphoserine
Modified residue16441Phosphoserine Ref.15
Modified residue17211Phosphoserine Ref.7 Ref.11
Modified residue17321Phosphoserine Ref.19
Modified residue25161Phosphoserine Ref.16
Modified residue27551Phosphoserine Ref.15
Modified residue28141Phosphothreonine Ref.11
Modified residue28411N6-acetyllysine Ref.25
Modified residue30331Phosphotyrosine By similarity
Modified residue30911N6-acetyllysine Ref.25
Modified residue33621Phosphotyrosine Ref.13
Modified residue34201N6-acetyllysine Ref.25
Modified residue40301Phosphothreonine Ref.11 Ref.16 Ref.19
Modified residue41551Phosphotyrosine Ref.13 Ref.22
Modified residue43821Phosphoserine Ref.11 Ref.19
Modified residue43841Phosphoserine Ref.11 Ref.12 Ref.19 Ref.21
Modified residue43851Phosphoserine Ref.5 Ref.11 Ref.19 Ref.21
Modified residue43861Phosphoserine Ref.6 Ref.7 Ref.11 Ref.17 Ref.19 Ref.21 Ref.24
Modified residue43891Phosphoserine Ref.7 Ref.16 Ref.19 Ref.21 Ref.24
Modified residue43901Phosphoserine
Modified residue43911Phosphoserine By similarity
Modified residue43921Phosphoserine Ref.19
Modified residue43931Phosphotyrosine Ref.19 Ref.21 Ref.22
Modified residue43961Phosphoserine Ref.12 Ref.16 Ref.19 Ref.21 Ref.24
Modified residue44001Phosphoserine Ref.21
Modified residue44021Phosphothreonine Ref.6
Modified residue44111Phosphothreonine Ref.11
Modified residue45391Phosphothreonine; by CDC2 By similarity
Modified residue46111Phosphotyrosine Ref.8 Ref.22
Modified residue46131Phosphoserine Ref.6 Ref.12 Ref.16 Ref.19 Ref.24
Modified residue46151Phosphotyrosine Ref.9 Ref.22
Modified residue46181Phosphoserine Ref.24
Modified residue46201Phosphoserine Ref.11 Ref.12
Modified residue46221Phosphoserine Ref.19
Modified residue46231Phosphothreonine Ref.6 Ref.19
Modified residue46261Phosphoserine Ref.19 Ref.24
Modified residue46281Phosphothreonine Ref.19
Modified residue46421Phosphoserine Ref.19
Modified residue46581Phosphoserine Ref.19
Modified residue46751Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 174174MVAGM…PAPAT → MSGEDAEVRAVSEDVSNGSS GSPSPGDTLPWNLGKTQRSR RSGGGAGSNGSVLDPAERAV IRIA in isoform 2 and isoform 3.
VSP_005030
Alternative sequence1 – 174174MVAGM…PAPAT → MSQHQLRVPQPEGLGRKRTS SEDNLYLAVLRASEGKK in isoform 4.
VSP_023510
Alternative sequence1 – 169169Missing in isoform 7.
VSP_037100
Alternative sequence1 – 159159Missing in isoform 8.
VSP_037101
Alternative sequence1 – 151151Missing in isoform 9.
VSP_037102
Alternative sequence1 – 137137Missing in isoform 5.
VSP_037103
Alternative sequence1 – 133133Missing in isoform 6.
VSP_037104
Alternative sequence134 – 17441TEEQR…PAPAT → MSGAGGAFASPREVLLERPC WLDGGCEPARRGYLYQQLCC V in isoform 6.
VSP_037105
Alternative sequence138 – 17437RVYRR…PAPAT → MEPSGSLFPSLVVVGHVVTL AAVWHWRRGRRWAQDEQ in isoform 5.
VSP_037106
Alternative sequence152 – 17423TPVVP…PAPAT → MAGPLPDEQDFIQAYEEVRE KYK in isoform 9.
VSP_037107
Alternative sequence160 – 17415QRTLA…PAPAT → MDPSRAIQNEISSLK in isoform 8.
VSP_037108
Alternative sequence170 – 1745PAPAT → MKIVP in isoform 7.
VSP_037109
Alternative sequence409 – 4124Missing in isoform 3.
VSP_005031
Natural variant4291L → LL in MD-EBS. Ref.29
VAR_011336
Natural variant6411A → V: dbSNP rs11136336.
VAR_053585
Natural variant1003 – 10053Missing in MD-EBS.
VAR_011337
Natural variant13211L → V: dbSNP rs3135109. Ref.2
VAR_060088
Natural variant13861R → Q: dbSNP rs11136334.
VAR_060089
Natural variant14591H → R: dbSNP rs55895668.
VAR_062133
Natural variant21101R → W in O-EBS. Ref.30
VAR_015817
Natural variant21501R → W: dbSNP rs34893635.
VAR_053586
Natural variant21941A → V: dbSNP rs7002002.
VAR_053587
Natural variant27911S → P: dbSNP rs7833924.
VAR_053588
Natural variant28211R → W: dbSNP rs35723243.
VAR_053589
Natural variant29691R → H: dbSNP rs6558407.
VAR_053590
Natural variant31621V → I: dbSNP rs35027700.
VAR_053591
Natural variant31711A → V: dbSNP rs35858667.
VAR_053592
Natural variant34861T → M: dbSNP rs34725742.
VAR_053593
Natural variant34901G → A: dbSNP rs35261863.
VAR_053594

Experimental info

Sequence conflict711Y → F in CAA91196. Ref.1
Sequence conflict941P → A in CAA91196. Ref.1
Sequence conflict1391V → L in CAA91196. Ref.1
Sequence conflict1851F → S in CAA91196. Ref.1
Sequence conflict2591N → D in AAB05427. Ref.2
Sequence conflict2591N → D in AAB05428. Ref.2
Sequence conflict5501N → H in CAA91196. Ref.1
Sequence conflict5601V → I in CAA91196. Ref.1
Sequence conflict7061R → Q in CAA91196. Ref.1
Sequence conflict8861Y → N in CAA91196. Ref.1
Sequence conflict10021A → V in CAA91196. Ref.1
Sequence conflict13091V → L in AAB05427. Ref.2
Sequence conflict13091V → L in AAB05428. Ref.2
Sequence conflict13341V → L in AAB05427. Ref.2
Sequence conflict13341V → L in AAB05428. Ref.2
Sequence conflict15341M → I in CAA91196. Ref.1
Sequence conflict16621A → T in AAB05427. Ref.2
Sequence conflict16621A → T in AAB05428. Ref.2
Sequence conflict1688 – 16903RLR → WLC in CAA91196. Ref.1
Sequence conflict17671E → Q in CAA91196. Ref.1
Sequence conflict17891A → L in CAA91196. Ref.1
Sequence conflict19101R → K in CAA91196. Ref.1
Sequence conflict21541K → N in AAB05427. Ref.2
Sequence conflict21541K → N in AAB05428. Ref.2
Sequence conflict21541K → N in CAA65765. Ref.2
Sequence conflict21541K → N in AAR95680. Ref.3
Sequence conflict21541K → N in AAR95682. Ref.3
Sequence conflict21541K → N in AAR95683. Ref.3
Sequence conflict21601R → S in CAA91196. Ref.1
Sequence conflict22151Q → R in CAA91196. Ref.1
Sequence conflict22441S → A in CAA91196. Ref.1
Sequence conflict22441S → A in AAB05427. Ref.2
Sequence conflict22441S → A in AAB05428. Ref.2
Sequence conflict22441S → A in CAA65765. Ref.2
Sequence conflict30271K → E in AAB05427. Ref.2
Sequence conflict30271K → E in AAB05428. Ref.2
Sequence conflict33101A → E in CAA91196. Ref.1
Sequence conflict33611L → F in CAA91196. Ref.1
Sequence conflict34081L → F in CAA91196. Ref.1
Sequence conflict34471A → S in CAA91196. Ref.1
Sequence conflict35311A → G in CAA91196. Ref.1
Sequence conflict35801S → R in CAA91196. Ref.1
Sequence conflict35891Q → K in CAA91196. Ref.1
Sequence conflict35961Q → E in CAA91196. Ref.1
Sequence conflict36161H → N in CAA91196. Ref.1
Sequence conflict36861A → V in CAA91196. Ref.1
Sequence conflict37861A → G in CAA91196. Ref.1
Sequence conflict38081R → K in CAA91196. Ref.1
Sequence conflict38161A → G in CAA91196. Ref.1
Sequence conflict38211C → F in CAA91196. Ref.1
Sequence conflict39151Q → K in CAA91196. Ref.1
Sequence conflict39991R → K in CAA91196. Ref.1
Sequence conflict40071T → S in CAA91196. Ref.1
Sequence conflict44671F → L in CAA91196. Ref.1

Secondary structure

1 ............................................. 4684
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Plectin-6) [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: 04772E4F70A304C8

FASTA4,684531,791
        10         20         30         40         50         60 
MVAGMLMPRD QLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMASLRARGL 

        70         80         90        100        110        120 
VRETFAWCHF YWYLTNEGIA HLRQYLHLPP EIVPASLQRV RRPVAMVMPA RRTPHVQAVQ 

       130        140        150        160        170        180 
GPLGSPPKRG PLPTEEQRVY RRKELEEVSP ETPVVPATTQ RTLARPGPEP APATDERDRV 

       190        200        210        220        230        240 
QKKTFTKWVN KHLIKAQRHI SDLYEDLRDG HNLISLLEVL SGDSLPREKG RMRFHKLQNV 

       250        260        270        280        290        300 
QIALDYLRHR QVKLVNIRND DIADGNPKLT LGLIWTIILH FQISDIQVSG QSEDMTAKEK 

       310        320        330        340        350        360 
LLLWSQRMVE GYQGLRCDNF TSSWRDGRLF NAIIHRHKPL LIDMNKVYRQ TNLENLDQAF 

       370        380        390        400        410        420 
SVAERDLGVT RLLDPEDVDV PQPDEKSIIT YVSSLYDAMP RVPDVQDGVR ANELQLRWQE 

       430        440        450        460        470        480 
YRELVLLLLQ WMRHHTAAFE ERRFPSSFEE IEILWSQFLK FKEMELPAKE ADKNRSKGIY 

       490        500        510        520        530        540 
QSLEGAVQAG QLKVPPGYHP LDVEKEWGKL HVAILEREKQ LRSEFERLEC LQRIVTKLQM 

       550        560        570        580        590        600 
EAGLCEEQLN QADALLQSDV RLLAAGKVPQ RAGEVERDLD KADSMIRLLF NDVQTLKDGR 

       610        620        630        640        650        660 
HPQGEQMYRR VYRLHERLVA IRTEYNLRLK AGVAAPATQV AQVTLQSVQR RPELEDSTLR 

       670        680        690        700        710        720 
YLQDLLAWVE ENQHRVDGAE WGVDLPSVEA QLGSHRGLHQ SIEEFRAKIE RARSDEGQLS 

       730        740        750        760        770        780 
PATRGAYRDC LGRLDLQYAK LLNSSKARLR SLESLHSFVA AATKELMWLN EKEEEEVGFD 

       790        800        810        820        830        840 
WSDRNTNMTA KKESYSALMR ELELKEKKIK ELQNAGDRLL REDHPARPTV ESFQAALQTQ 

       850        860        870        880        890        900 
WSWMLQLCCC IEAHLKENAA YFQFFSDVRE AEGQLQKLQE ALRRKYSCDR SATVTRLEDL 

       910        920        930        940        950        960 
LQDAQDEKEQ LNEYKGHLSG LAKRAKAVVQ LKPRHPAHPM RGRLPLLAVC DYKQVEVTVH 

       970        980        990       1000       1010       1020 
KGDECQLVGP AQPSHWKVLS SSGSEAAVPS VCFLVPPPNQ EAQEAVTRLE AQHQALVTLW 

      1030       1040       1050       1060       1070       1080 
HQLHVDMKSL LAWQSLRRDV QLIRSWSLAT FRTLKPEEQR QALHSLELHY QAFLRDSQDA 

      1090       1100       1110       1120       1130       1140 
GGFGPEDRLM AEREYGSCSH HYQQLLQSLE QGAQEESRCQ RCISELKDIR LQLEACETRT 

      1150       1160       1170       1180       1190       1200 
VHRLRLPLDK EPARECAQRI AEQQKAQAEV EGLGKGVARL SAEAEKVLAL PEPSPAAPTL 

      1210       1220       1230       1240       1250       1260 
RSELELTLGK LEQVRSLSAI YLEKLKTISL VIRGTQGAEE VLRAHEEQLK EAQAVPATLP 

      1270       1280       1290       1300       1310       1320 
ELEATKASLK KLRAQAEAQQ PTFDALRDEL RGAQEVGERL QQRHGERDVE VERWRERVAQ 

      1330       1340       1350       1360       1370       1380 
LLERWQAVLA QTDVRQRELE QLGRQLRYYR ESADPLGAWL QDARRRQEQI QAMPLADSQA 

      1390       1400       1410       1420       1430       1440 
VREQLRQEQA LLEEIERHGE KVEECQRFAK QYINAIKDYE LQLVTYKAQL EPVASPAKKP 

      1450       1460       1470       1480       1490       1500 
KVQSGSESVI QEYVDLRTHY SELTTLTSQY IKFISETLRR MEEEERLAEQ QRAEERERLA 

      1510       1520       1530       1540       1550       1560 
EVEAALEKQR QLAEAHAQAK AQAEREAKEL QQRMQEEVVR REEAAVDAQQ QKRSIQEELQ 

      1570       1580       1590       1600       1610       1620 
QLRQSSEAEI QAKARQAEAA ERSRLRIEEE IRVVRLQLEA TERQRGGAEG ELQALRARAE 

      1630       1640       1650       1660       1670       1680 
EAEAQKRQAQ EEAERLRRQV QDESQRKRQA EVELASRVKA EAEAAREKQR ALQALEELRL 

      1690       1700       1710       1720       1730       1740 
QAEEAERRLR QAEVERARQV QVALETAQRS AEAELQSKRA SFAEKTAQLE RSLQEEHVAV 

      1750       1760       1770       1780       1790       1800 
AQLREEAERR AQQQAEAERA REEAERELER WQLKANEALR LRLQAEEVAQ QKSLAQAEAE 

      1810       1820       1830       1840       1850       1860 
KQKEEAEREA RRRGKAEEQA VRQRELAEQE LEKQRQLAEG TAQQRLAAEQ ELIRLRAETE 

      1870       1880       1890       1900       1910       1920 
QGEQQRQLLE EELARLQREA AAATQKRQEL EAELAKVRAE MEVLLASKAR AEEESRSTSE 

      1930       1940       1950       1960       1970       1980 
KSKQRLEAEA GRFRELAEEA ARLRALAEEA KRQRQLAEED AARQRAEAER VLAEKLAAIG 

      1990       2000       2010       2020       2030       2040 
EATRLKTEAE IALKEKEAEN ERLRRLAEDE AFQRRRLEEQ AAQHKADIEE RLAQLRKASD 

      2050       2060       2070       2080       2090       2100 
SELERQKGLV EDTLRQRRQV EEEILALKAS FEKAAAGKAE LELELGRIRS NAEDTLRSKE 

      2110       2120       2130       2140       2150       2160 
QAELEAARQR QLAAEEERRR REAEERVQKS LAAEEEAARQ RKAALEEVER LKAKVEEARR 

      2170       2180       2190       2200       2210       2220 
LRERAEQESA RQLQLAQEAA QKRLQAEEKA HAFAVQQKEQ ELQQTLQQEQ SVLDQLRGEA 

      2230       2240       2250       2260       2270       2280 
EAARRAAEEA EEARVQAERE AAQSRRQVEE AERLKQSAEE QAQARAQAQA AAEKLRKEAE 

      2290       2300       2310       2320       2330       2340 
QEAARRAQAE QAALRQKQAA DAEMEKHKKF AEQTLRQKAQ VEQELTTLRL QLEETDHQKN 

      2350       2360       2370       2380       2390       2400 
LLDEELQRLK AEATEAARQR SQVEEELFSV RVQMEELSKL KARIEAENRA LILRDKDNTQ 

      2410       2420       2430       2440       2450       2460 
RFLQEEAEKM KQVAEEAARL SVAAQEAARL RQLAEEDLAQ QRALAEKMLK EKMQAVQEAT 

      2470       2480       2490       2500       2510       2520 
RLKAEAELLQ QQKELAQEQA RRLQEDKEQM AQQLAEETQG FQRTLEAERQ RQLEMSAEAE 

      2530       2540       2550       2560       2570       2580 
RLKLRVAEMS RAQARAEEDA QRFRKQAEEI GEKLHRTELA TQEKVTLVQT LEIQRQQSDH 

      2590       2600       2610       2620       2630       2640 
DAERLREAIA ELEREKEKLQ QEAKLLQLKS EEMQTVQQEQ LLQETQALQQ SFLSEKDSLL 

      2650       2660       2670       2680       2690       2700 
QRERFIEQEK AKLEQLFQDE VAKAQQLREE QQRQQQQMEQ ERQRLVASME EARRRQHEAE 

      2710       2720       2730       2740       2750       2760 
EGVRRKQEEL QQLEQQRRQQ EELLAEENQR LREQLQLLEE QHRAALAHSE EVTASQVAAT 

      2770       2780       2790       2800       2810       2820 
KTLPNGRDAL DGPAAEAEPE HSFDGLRRKV SAQRLQEAGI LSAEELQRLA QGHTTVDELA 

      2830       2840       2850       2860       2870       2880 
RREDVRHYLQ GRSSIAGLLL KATNEKLSVY AALQRQLLSP GTALILLEAQ AASGFLLDPV 

      2890       2900       2910       2920       2930       2940 
RNRRLTVNEA VKEGVVGPEL HHKLLSAERA VTGYKDPYTG QQISLFQAMQ KGLIVREHGI 

      2950       2960       2970       2980       2990       3000 
RLLEAQIATG GVIDPVHSHR VPVDVAYRRG YFDEEMNRVL ADPSDDTKGF FDPNTHENLT 

      3010       3020       3030       3040       3050       3060 
YLQLLERCVE DPETGLCLLP LTDKAAKGGE LVYTDSEARD VFEKATVSAP FGKFQGKTVT 

      3070       3080       3090       3100       3110       3120 
IWEIINSEYF TAEQRRDLLR QFRTGRITVE KIIKIIITVV EEQEQKGRLC FEGLRSLVPA 

      3130       3140       3150       3160       3170       3180 
AELLESRVID RELYQQLQRG ERSVRDVAEV DTVRRALRGA NVIAGVWLEE AGQKLSIYNA 

      3190       3200       3210       3220       3230       3240 
LKKDLLPSDM AVALLEAQAG TGHIIDPATS ARLTVDEAVR AGLVGPEFHE KLLSAEKAVT 

      3250       3260       3270       3280       3290       3300 
GYRDPYTGQS VSLFQALKKG LIPREQGLRL LDAQLSTGGI VDPSKSHRVP LDVACARGCL 

      3310       3320       3330       3340       3350       3360 
DEETSRALSA PRADAKAYSD PSTGEPATYG ELQQRCRPDQ LTGLSLLPLS EKAARARQEE 

      3370       3380       3390       3400       3410       3420 
LYSELQARET FEKTPVEVPV GGFKGRTVTV WELISSEYFT AEQRQELLRQ FRTGKVTVEK 

      3430       3440       3450       3460       3470       3480 
VIKILITIVE EVETLRQERL SFSGLRAPVP ASELLASGVL SRAQFEQLKD GKTTVKDLSE 

      3490       3500       3510       3520       3530       3540 
LGSVRTLLQG SGCLAGIYLE DTKEKVSIYE AMRRGLLRAT TAALLLEAQA ATGFLVDPVR 

      3550       3560       3570       3580       3590       3600 
NQRLYVHEAV KAGVVGPELH EQLLSAEKAV TGYRDPYSGS TISLFQAMQK GLVLRQHGIR 

      3610       3620       3630       3640       3650       3660 
LLEAQIATGG IIDPVHSHRV PVDVAYQRGY FSEEMNRVLA DPSDDTKGFF DPNTHENLTY 

      3670       3680       3690       3700       3710       3720 
RQLLERCVED PETGLRLLPL KGAEKAEVVE TTQVYTEEET RRAFEETQID IPGGGSHGGS 

      3730       3740       3750       3760       3770       3780 
TMSLWEVMQS DLIPEEQRAQ LMADFQAGRV TKERMIIIII EIIEKTEIIR QQGLASYDYV 

      3790       3800       3810       3820       3830       3840 
RRRLTAEDLF EARIISLETY NLLREGTRSL REALEAESAW CYLYGTGSVA GVYLPGSRQT 

      3850       3860       3870       3880       3890       3900 
LSIYQALKKG LLSAEVARLL LEAQAATGFL LDPVKGERLT VDEAVRKGLV GPELHDRLLS 

      3910       3920       3930       3940       3950       3960 
AERAVTGYRD PYTEQTISLF QAMKKELIPT EEALRLLDAQ LATGGIVDPR LGFHLPLEVA 

      3970       3980       3990       4000       4010       4020 
YQRGYLNKDT HDQLSEPSEV RSYVDPSTDE RLSYTQLLRR CRRDDGTGQL LLPLSDARKL 

      4030       4040       4050       4060       4070       4080 
TFRGLRKQIT MEELVRSQVM DEATALQLRE GLTSIEEVTK NLQKFLEGTS CIAGVFVDAT 

      4090       4100       4110       4120       4130       4140 
KERLSVYQAM KKGIIRPGTA FELLEAQAAT GYVIDPIKGL KLTVEEAVRM GIVGPEFKDK 

      4150       4160       4170       4180       4190       4200 
LLSAERAVTG YKDPYSGKLI SLFQAMKKGL ILKDHGIRLL EAQIATGGII DPEESHRLPV 

      4210       4220       4230       4240       4250       4260 
EVAYKRGLFD EEMNEILTDP SDDTKGFFDP NTEENLTYLQ LMERCITDPQ TGLCLLPLKE 

      4270       4280       4290       4300       4310       4320 
KKRERKTSSK SSVRKRRVVI VDPETGKEMS VYEAYRKGLI DHQTYLELSE QECEWEEITI 

      4330       4340       4350       4360       4370       4380 
SSSDGVVKSM IIDRRSGRQY DIDDAIAKNL IDRSALDQYR AGTLSITEFA DMLSGNAGGF 

      4390       4400       4410       4420       4430       4440 
RSRSSSVGSS SSYPISPAVS RTQLASWSDP TEETGPVAGI LDTETLEKVS ITEAMHRNLV 

      4450       4460       4470       4480       4490       4500 
DNITGQRLLE AQACTGGIID PSTGERFPVT DAVNKGLVDK IMVDRINLAQ KAFCGFEDPR 

      4510       4520       4530       4540       4550       4560 
TKTKMSAAQA LKKGWLYYEA GQRFLEVQYL TGGLIEPDTP GRVPLDEALQ RGTVDARTAQ 

      4570       4580       4590       4600       4610       4620 
KLRDVGAYSK YLTCPKTKLK ISYKDALDRS MVEEGTGLRL LEAAAQSTKG YYSPYSVSGS 

      4630       4640       4650       4660       4670       4680 
GSTAGSRTGS RTGSRAGSRR GSFDATGSGF SMTFSSSSYS SSGYGRRYAS GSSASLGGPE 


SAVA

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Isoform 2 (Plectin-1).

Checksum: 7EAEA5A83DEF52EA
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FASTA4,574518,473
Isoform 3.

Checksum: A0AF260B8C095C8D
Show »

FASTA4,570518,032
Isoform 4 (Plectin-11).

Checksum: 0A1A2AB2E557110A
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FASTA4,547516,198
Isoform 5 (Plectin-8).

Checksum: 0EC98F109B723779
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FASTA4,547516,276
Isoform 6 (Plectin-10).

Checksum: C2E0FDA51BC17BF2
Show »

FASTA4,551516,479
Isoform 7 (Plectin-7).

Checksum: C8701AD6D1C1B26E
Show »

FASTA4,515512,604
Isoform 8 (Plectin-3).

Checksum: 37A4DFAB46C3B4DD
Show »

FASTA4,525513,706
Isoform 9 (Plectin-2).

Checksum: 5D6382389A66B955
Show »

FASTA4,533514,775

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References

« Hide 'large scale' references
[1]"Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24)."
Liu C.-G., Maercker C., Castanon M.J., Hauptmann R., Wiche G.
Proc. Natl. Acad. Sci. U.S.A. 93:4278-4283(1996) [PubMed: 8633055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[2]"Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA cloning and genomic organization."
McLean W.H.I., Pulkkinen L., Smith F.J.D., Rugg E.L., Lane E.B., Bullrich F., Burgeson R.E., Amano S., Hudson D.L., Owaribe K., McGrath J.A., McMillan J.R., Eady R.A.J., Leigh I.M., Christiano A.M., Uitto J.
Genes Dev. 10:1724-1735(1996) [PubMed: 8698233] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), DISEASE, VARIANT VAL-1321.
[3]"Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation."
Zhang T., Haws P., Wu Q.
Genome Res. 14:79-89(2004) [PubMed: 14672974] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7; 8 AND 9).
[4]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed: 16421571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 14-21; 209-227; 237-248; 301-316; 329-336; 350-365; 372-417; 510-517; 588-597; 631-675; 697-706; 714-724; 734-740; 751-764; 857-869; 897-908; 927-934; 1029-1037; 1045-1052; 1076-1088; 1131-1139; 1166-1175; 1187-1210; 1216-1224; 1227-1243; 1251-1266; 1274-1291; 1318-1335; 1338-1344; 1351-1364; 1366-1382; 1411-1438; 1473-1479; 1499-1508; 1554-1563; 1596-1603; 1606-1616; 1628-1638; 1649-1657; 1671-1679; 1699-1709; 1732-1744; 1783-1792; 1825-1833; 1846-1854; 1867-1875; 1888-1908; 1976-1994; 2006-2014; 2048-2055; 2058-2068; 2079-2087; 2098-2108; 2130-2139; 2142-2150; 2172-2182; 2199-2217; 2310-2316; 2319-2329; 2340-2348; 2361-2379; 2402-2409; 2420-2429; 2432-2442; 2462-2473; 2483-2503; 2512-2521; 2565-2575; 2587-2594; 2651-2663; 2685-2693; 2705-2761; 2768-2787; 2795-2821; 2833-2841; 2847-2881; 2885-2903; 2942-2968; 2979-3007; 3028-3039; 3045-3053; 3095-3106; 3109-3127; 3132-3139; 3146-3154; 3175-3183; 3213-3231; 3244-3259; 3270-3285; 3289-3297; 3317-3335; 3356-3368; 3374-3384; 3424-3436; 3447-3469; 3477-3485; 3506-3513; 3519-3540; 3544-3568; 3601-3637; 3648-3661; 3667-3676; 3686-3702; 3739-3749; 3771-3781; 3784-3804; 3839-3878; 3887-3897; 3926-3963; 3969-3999; 4004-4018; 4027-4060; 4084-4091; 4122-4138; 4159-4167; 4179-4205; 4278-4296; 4339-4348; 4354-4360; 4384-4401; 4429-4447; 4467-4475; 4492-4500; 4543-4551; 4590-4627 AND 4668-4684, PHOSPHORYLATION AT SER-4385, MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[6]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; SER-1435; SER-4386; THR-4402; SER-4613 AND THR-4623, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1721; SER-4386 AND SER-4389, MASS SPECTROMETRY.
[8]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4611, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4615, MASS SPECTROMETRY.
[10]"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.
Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782, MASS SPECTROMETRY.
Tissue: Hepatocyte.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-1435; SER-1721; THR-2814; THR-4030; SER-4382; SER-4384; SER-4385; SER-4386; THR-4411 AND SER-4620, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435; SER-4384; SER-4396; SER-4613 AND SER-4620, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3362 AND TYR-4155, MASS SPECTROMETRY.
[14]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM 4), MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1644 AND SER-2755, MASS SPECTROMETRY.
[16]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-720; SER-1435; SER-2516; THR-4030; SER-4389; SER-4396; SER-4613 AND SER-4675, MASS SPECTROMETRY.
[17]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4386, MASS SPECTROMETRY.
[18]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-720 AND SER-1435, MASS SPECTROMETRY.
[19]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-149; SER-720; SER-1435; SER-1732; THR-4030; SER-4382; SER-4384; SER-4385; SER-4386; SER-4389; SER-4392; TYR-4393; SER-4396; SER-4613; SER-4622; THR-4623; SER-4626; THR-4628; SER-4642 AND SER-4658, MASS SPECTROMETRY.
[20]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1435; SER-4384; SER-4385; SER-4386; SER-4389; TYR-4393; SER-4396 AND SER-4400, MASS SPECTROMETRY.
[22]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26; (ISOFORM 4) TYR-4155; TYR-4393; TYR-4611 AND TYR-4615, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[23]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720; SER-1435; SER-1444; THR-4030; SER-4384; SER-4389; SER-4390; THR-4402 AND SER-4626, MASS SPECTROMETRY.
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4386; SER-4389; SER-4396; SER-4613; SER-4618 AND SER-4626, MASS SPECTROMETRY.
Tissue: T-cell.
[25]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187; LYS-2841; LYS-3091 AND LYS-3420, MASS SPECTROMETRY.
[26]"The structure of a tandem pair of spectrin repeats of plectin reveals a modular organization of the plakin domain."
Sonnenberg A., Rojas A.M., de Pereda J.M.
J. Mol. Biol. 368:1379-1391(2007) [PubMed: 17397861] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 409-640.
[27]"Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4."
Garcia-Alvarez B., Bobkov A., Sonnenberg A., de Pereda J.M.
Structure 11:615-625(2003) [PubMed: 12791251] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 159-403.
[28]"Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy."
Pulkkinen L., Smith F.J.D., Shimizu H., Murata S., Yaoita H., Hachisuka H., Nishikawa T., McLean W.H.I., Uitto J.
Hum. Mol. Genet. 5:1539-1546(1996) [PubMed: 8894687] [Abstract]
Cited for: VARIANT MD-EBS 1003-GLN--ALA-1005 DEL.
[29]"A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency."
Bauer J.W., Rouan F., Kofler B., Rezniczek G.A., Kornacker I., Muss W., Hametner R., Klausegger A., Huber A., Pohla-Gubo G., Wiche G., Uitto J., Hintner H.
Am. J. Pathol. 158:617-625(2001) [PubMed: 11159198] [Abstract]
Cited for: VARIANT MD-EBS LEU-429 INS.
[30]"A site-specific plectin mutation causes dominant epidermolysis bullosa simplex Ogna: two identical de novo mutations."
Koss-Harnes D., Hoeyheim B., Anton-Lamprecht I., Gjesti A., Joergensen R.S., Jahnsen F.L., Olaisen B., Wiche G., Gedde-Dahl T. Jr.
J. Invest. Dermatol. 118:87-93(2002) [PubMed: 11851880] [Abstract]
Cited for: VARIANT O-EBS TRP-2110.
[31]"Identification of a lethal form of epidermolysis bullosa simplex associated with a homozygous genetic mutation in plectin."
Charlesworth A., Gagnoux-Palacios L., Bonduelle M., Ortonne J.-P., De Raeve L., Meneguzzi G.
J. Invest. Dermatol. 121:1344-1348(2003) [PubMed: 14675180] [Abstract]
Cited for: INVOLVEMENT IN EBS-PA.
+Additional computationally mapped references.

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Web resources

Wikipedia

Plectin entry

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z54367 Genomic DNA. Translation: CAA91196.1.
U53204 mRNA. Translation: AAB05427.1.
U63610, U63609 Genomic DNA. Translation: AAB05428.1.
X97053 mRNA. Translation: CAA65765.1.
AY480044 mRNA. Translation: AAR95677.1.
AY480045 mRNA. Translation: AAR95678.1.
AY480046 mRNA. Translation: AAR95679.1.
AY480047 mRNA. Translation: AAR95680.1.
AY480048 mRNA. Translation: AAR95681.1.
AY480049 mRNA. Translation: AAR95682.1.
AY480050 mRNA. Translation: AAR95683.1.
AY480051 mRNA. Translation: AAR95684.1.
AC109322 Genomic DNA. No translation available.
IPIIPI00014898.
IPI00186711.
IPI00398002.
IPI00398775.
IPI00398776.
IPI00398777.
IPI00398778.
IPI00398779.
IPI00420096.
PIRA59404. C59404.
G02520.
RefSeqNP_000436.2.
NP_958780.1.
NP_958781.1.
NP_958782.1.
NP_958783.1.
NP_958784.1.
NP_958785.1.
NP_958786.1.
UniGeneHs.434248

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MB8X-ray2.15A175-403[»]
2ODUX-ray2.30A410-640[»]
2ODVX-ray2.05A410-640[»]
3F7PX-ray2.75A/B175-403[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ15149. 3 interactions.
STRINGQ15149.

PTM databases

PhosphoSiteQ15149.

Proteomic databases

PRIDEQ15149.

Genome annotation databases

EnsemblENST00000322810; ENSP00000323856; ENSG00000178209; Homo sapiens. [Genome view]
GeneID5339.
KEGGhsa:5339.
UCSCuc003zab.1. human.

Organism-specific databases

CTD5339.
GeneCardsGC08M145061.
GC08M145062.
H-InvDBHIX0055497.
HGNCHGNC:9069. PLEC1.
HPACAB003847.
MIM131950. phenotype.
226670. phenotype.
601282. gene.
612138. phenotype.
Orphanet257. Epidermolysis bullosa simplex - limb girdle muscular dystrophy.
158684. Epidermolysis bullosa simplex - pyloric atresia.
79401. Epidermolysis bullosa simplex, Ogna type.
304. Epidermolysis bullosa, epidermolytic.
PharmGKBPA33399.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07394.
HOVERGENQ15149.
InParanoidQ15149.
OMADVFEKAT.
PhylomeDBQ15149.

Enzyme and pathway databases

ReactomeREACT_20676. Cell junction organization.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ15149.
BgeeQ15149.
CleanExHS_PLEC1.
GenevestigatorQ15149.
GermOnlineENSG00000178209. Homo sapiens.

Family and domain databases

InterProIPR001589. Actinin_actin-bd_CS.
IPR016146. Calponin-homology.
IPR001715. Calponin_act_bd.
IPR015622. Plectin.
IPR001101. Plectin_repeat.
IPR005326. S10_plectin_N.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
Gene3DG3DSA:1.10.418.10. Calponin-homology. 2 hits.
PANTHERPTHR11915:SF52. Plectin. 1 hit.
PfamPF00307. CH. 2 hits.
PF00681. Plectin. 18 hits.
PF03501. S10_plectin. 1 hit.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00250. PLEC. 32 hits.
SM00150. SPEC. 7 hits.
[Graphical view]
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio20680.
SOURCESearch...

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Entry information

Entry namePLEC1_HUMAN
AccessionPrimary (citable) accession number: Q15149
Secondary accession number(s): Q15148 expand/collapse secondary AC list , Q16640, Q6S376, Q6S377, Q6S378, Q6S379, Q6S380, Q6S381, Q6S382, Q6S383
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 14, 2008
Last modified: February 9, 2010
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents