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Protein

Plectin

Gene

Plec

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. May be involved not only in the cross-linking and stabilization of cytoskeletal intermediate filaments network, but also in the regulation of their dynamics.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-2022090. Assembly of collagen fibrils and other multimeric structures.
R-MMU-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-MMU-446107. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Plectin
Short name:
PCN
Short name:
PLTN
Alternative name(s):
Plectin-1
Plectin-6
Gene namesi
Name:Plec
Synonyms:Plec1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1277961. Plec.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: UniProtKB
  • contractile fiber Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • hemidesmosome Source: UniProtKB
  • intermediate filament cytoskeleton Source: MGI
  • sarcolemma Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 46914691PlectinPRO_0000078136Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei728 – 7281PhosphoserineCombined sources
Modified residuei823 – 8231PhosphothreonineCombined sources
Modified residuei1055 – 10551PhosphoserineCombined sources
Modified residuei1443 – 14431PhosphoserineBy similarity
Modified residuei1729 – 17291PhosphoserineBy similarity
Modified residuei1733 – 17331N6-acetyllysineCombined sources
Modified residuei2639 – 26391PhosphoserineBy similarity
Modified residuei2644 – 26441N6-acetyllysineCombined sources
Modified residuei2781 – 27811PhosphoserineBy similarity
Modified residuei2788 – 27881PhosphotyrosineCombined sources
Modified residuei2809 – 28091PhosphoserineBy similarity
Modified residuei2893 – 28931PhosphothreonineBy similarity
Modified residuei3040 – 30401PhosphotyrosineCombined sources
Modified residuei3060 – 30601N6-acetyllysineCombined sources
Modified residuei3098 – 30981N6-acetyllysineBy similarity
Modified residuei3369 – 33691PhosphotyrosineCombined sources
Modified residuei3427 – 34271N6-acetyllysineBy similarity
Modified residuei3792 – 37921PhosphothreonineBy similarity
Modified residuei3797 – 37971PhosphotyrosineCombined sources
Modified residuei4037 – 40371PhosphothreonineCombined sources
Modified residuei4061 – 40611PhosphoserineBy similarity
Modified residuei4389 – 43891PhosphoserineCombined sources
Modified residuei4391 – 43911PhosphoserineCombined sources
Modified residuei4392 – 43921PhosphoserineCombined sources
Modified residuei4393 – 43931PhosphoserineCombined sources
Modified residuei4396 – 43961PhosphoserineCombined sources
Modified residuei4397 – 43971PhosphoserineBy similarity
Modified residuei4398 – 43981PhosphoserineBy similarity
Modified residuei4399 – 43991PhosphoserineBy similarity
Modified residuei4400 – 44001PhosphotyrosineBy similarity
Modified residuei4403 – 44031PhosphoserineBy similarity
Modified residuei4413 – 44131PhosphoserineBy similarity
Modified residuei4418 – 44181PhosphothreonineBy similarity
Modified residuei4546 – 45461Phosphothreonine; by CDK1By similarity
Modified residuei4614 – 46141PhosphoserineBy similarity
Modified residuei4620 – 46201PhosphoserineCombined sources
Modified residuei4622 – 46221PhosphotyrosineCombined sources
Modified residuei4623 – 46231PhosphoserineBy similarity
Modified residuei4625 – 46251PhosphoserineCombined sources
Modified residuei4629 – 46291PhosphoserineCombined sources
Modified residuei4630 – 46301PhosphothreonineCombined sources
Modified residuei4633 – 46331PhosphoserineCombined sources
Modified residuei4649 – 46491PhosphoserineCombined sources
Modified residuei4682 – 46821PhosphoserineBy similarity
Isoform PLEC-1A (identifier: Q9QXS1-3)
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei26 – 261PhosphotyrosineCombined sources

Post-translational modificationi

Phosphorylated by CDK1; regulates dissociation from intermediate filaments during mitosis. Isoform PLEC-1A is phosphorylated on Ser-21. Isoform PLEC-1A is phosphorylated on Tyr-26.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9QXS1.
MaxQBiQ9QXS1.
PaxDbiQ9QXS1.
PeptideAtlasiQ9QXS1.
PRIDEiQ9QXS1.

PTM databases

iPTMnetiQ9QXS1.
PhosphoSiteiQ9QXS1.
SwissPalmiQ9QXS1.

Expressioni

Tissue specificityi

Detected in eye lens fiber cells (at protein level) (PubMed:21745462). Expressed at high levels in lung, brain, small intestine, muscle, heart and skin with lower levels found in kidney, liver, uterus, spleen and salivary gland (PubMed:10556294).2 Publications

Gene expression databases

BgeeiQ9QXS1.
CleanExiMM_PLEC1.
ExpressionAtlasiQ9QXS1. baseline and differential.
GenevisibleiQ9QXS1. MM.

Interactioni

Subunit structurei

Homodimer or homotetramer (By similarity). Interacts (via actin-binding domain) with SYNE3 (PubMed:16330710). Interacts (via CH 1 domain) with VIM (via rod region) (PubMed:15128297). Interacts (via N-terminus) with DST isoform 2 (via N-terminus) (PubMed:19932097). Interacts with FER (PubMed:12200133). Interacts with TOR1A (PubMed:18827015). Interacts with ANK3 (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462).By similarity6 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202243. 11 interactions.
DIPiDIP-32004N.
IntActiQ9QXS1. 6 interactions.
MINTiMINT-1867366.
STRINGi10090.ENSMUSP00000073124.

Structurei

Secondary structure

1
4691
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi181 – 19919Combined sources
Helixi205 – 2073Combined sources
Turni214 – 2207Combined sources
Helixi222 – 23211Combined sources
Helixi244 – 26017Combined sources
Helixi270 – 2745Combined sources
Helixi278 – 29215Combined sources
Helixi294 – 2963Combined sources
Helixi308 – 31912Combined sources
Turni320 – 3223Combined sources
Helixi333 – 3353Combined sources
Helixi339 – 34810Combined sources
Helixi350 – 3523Combined sources
Helixi355 – 3606Combined sources
Helixi363 – 37816Combined sources
Helixi386 – 3894Combined sources
Beta strandi390 – 3934Combined sources
Helixi396 – 40813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SH5X-ray2.00A/B181-417[»]
1SH6X-ray2.00A181-417[»]
4Q57X-ray1.80B181-411[»]
ProteinModelPortaliQ9QXS1.
SMRiQ9QXS1. Positions 5-101, 181-411, 424-641, 661-1033, 3448-3688, 4028-4267, 4410-4613.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QXS1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 411231Actin-bindingAdd
BLAST
Domaini185 – 293109CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini306 – 408103CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati653 – 72775Spectrin 1Add
BLAST
Repeati748 – 83285Spectrin 2Add
BLAST
Repeati845 – 93894Spectrin 3Add
BLAST
Repeati1323 – 1423101Spectrin 4Add
BLAST
Repeati2795 – 283238Plectin 1Add
BLAST
Repeati2833 – 287038Plectin 2Add
BLAST
Repeati2871 – 290838Plectin 3Add
BLAST
Repeati2909 – 294638Plectin 4Add
BLAST
Repeati2947 – 298438Plectin 5Add
BLAST
Repeati2988 – 302235Plectin 6Add
BLAST
Repeati3123 – 316038Plectin 7Add
BLAST
Repeati3161 – 319838Plectin 8Add
BLAST
Repeati3199 – 323638Plectin 9Add
BLAST
Repeati3237 – 327438Plectin 10Add
BLAST
Repeati3275 – 331238Plectin 11Add
BLAST
Repeati3315 – 335036Plectin 12Add
BLAST
Repeati3492 – 352938Plectin 13Add
BLAST
Repeati3530 – 356738Plectin 14Add
BLAST
Repeati3568 – 360538Plectin 15Add
BLAST
Repeati3606 – 364338Plectin 16Add
BLAST
Repeati3647 – 368135Plectin 17Add
BLAST
Repeati3827 – 386438Plectin 18Add
BLAST
Repeati3865 – 390238Plectin 19Add
BLAST
Repeati3903 – 394038Plectin 20Add
BLAST
Repeati3941 – 397838Plectin 21Add
BLAST
Repeati3982 – 401534Plectin 22Add
BLAST
Repeati4070 – 410738Plectin 23Add
BLAST
Repeati4108 – 414538Plectin 24Add
BLAST
Repeati4146 – 418338Plectin 25Add
BLAST
Repeati4184 – 422138Plectin 26Add
BLAST
Repeati4225 – 425935Plectin 27Add
BLAST
Repeati4272 – 431241Plectin 28Add
BLAST
Repeati4415 – 445238Plectin 29Add
BLAST
Repeati4453 – 449038Plectin 30Add
BLAST
Repeati4491 – 452838Plectin 31Add
BLAST
Repeati4529 – 456638Plectin 32Add
BLAST
Repeati4567 – 460438Plectin 33Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 14781478Globular 1By similarityAdd
BLAST
Regioni1479 – 27621284Central fibrous rod domainBy similarityAdd
BLAST
Regioni2763 – 46911929Globular 2By similarityAdd
BLAST
Regioni4257 – 430751Binding to intermediate filamentsBy similarityAdd
BLAST
Regioni4632 – 4647164 X 4 AA tandem repeats of G-S-R-XAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1477 – 1697221Sequence analysisAdd
BLAST
Coiled coili1729 – 27641036Sequence analysisAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the plakin or cytolinker family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 33 plectin repeats.Curated
Contains 4 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG0516. Eukaryota.
KOG3344. Eukaryota.
COG5045. LUCA.
COG5069. LUCA.
GeneTreeiENSGT00760000119163.
HOVERGENiHBG053616.
InParanoidiQ9QXS1.
KOiK10388.
OMAiYLNKDTH.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
3.90.1290.10. 7 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR030269. Plectin.
IPR001101. Plectin_repeat.
IPR005326. S10_plectin_N.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PANTHERiPTHR11915:SF247. PTHR11915:SF247. 4 hits.
PfamiPF00307. CH. 2 hits.
PF00681. Plectin. 18 hits.
PF03501. S10_plectin. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00250. PLEC. 35 hits.
SM00150. SPEC. 6 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 8 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]

Sequences (16)i

Sequence statusi: Complete.

This entry describes 16 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform PLEC-1,2A (identifier: Q9QXS1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVAGMLMPLD RLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR
60 70 80 90 100
AMASLKARGL VRETFAWCHF YWYLTNEGID HLRQYLHLPP EIVPASLQRV
110 120 130 140 150
RRPVAMVIPA RRRSPHVQTM QGPLGCPPKR GPLPAEDPAR EERQVYRRKE
160 170 180 190 200
REEGAPETPV VSATTVGTLA RPGPEPAPAT DERDRVQKKT FTKWVNKHLI
210 220 230 240 250
KHWRAEAQRH ISDLYEDLRD GHNLISLLEV LSGDSLPREK GRMRFHKLQN
260 270 280 290 300
VQIALDYLRH RQVKLVNIRN DDIADGNPKL TLGLIWTIIL HFQISDIQVS
310 320 330 340 350
GQSEDMTAKE KLLLWSQRMV EGYQGLRCDN FTTSWRDGRL FNAIIHRHKP
360 370 380 390 400
MLIDMNKVYR QTNLENLDQA FSVAERDLGV TRLLDPEDVD VPQPDEKSII
410 420 430 440 450
TYVSSLYDAM PRVPGAQDGV RANELQLRWQ EYRELVLLLL QWIRHHTAAF
460 470 480 490 500
EERKFPSSFE EIEILWCQFL KFKETELPAK EADKNRSKVI YQSLEGAVQA
510 520 530 540 550
GQLKIPPGYH PLDVEKEWGK LHVAILEREK QLRSEFERLE CLQRIVSKLQ
560 570 580 590 600
MEAGLCEEQL NQADALLQSD IRLLASGKVA QRAGEVERDL DKADGMIRLL
610 620 630 640 650
FNDVQTLKDG RHPQGEQMYR RVYRLHERLV AIRTEYNLRL KAGVGAPVTQ
660 670 680 690 700
VTLQSTQRRP ELEDSTLRYL QDLLAWVEEN QRRIDSAEWG VDLPSVEAQL
710 720 730 740 750
GSHRGMHQSI EEFRAKIERA RNDESQLSPA TRGAYRDCLG RLDLQYAKLL
760 770 780 790 800
NSSKARLRSL ESLHGFVAAA TKELMWLNEK EEEEVGFDWS DRNTNMAAKK
810 820 830 840 850
ESYSALMREL EMKEKKIKEI QNTGDRLLRE DHPARPTVES FQAALQTQWS
860 870 880 890 900
WMLQLCCCIE AHLKENTAYF QFFSDVREAE EQLQKLQETL RRKYSCDRTI
910 920 930 940 950
TVTRLEDLLQ DAQDEKEQLN EYKGHLSGLA KRAKAIVQLK PRNPAHPVRG
960 970 980 990 1000
HVPLIAVCDY KQVEVTVHKG DQCQLVGPAQ PSHWKVLSGS SSEAAVPSVC
1010 1020 1030 1040 1050
FLVPPPNQEA QEAVARLEAQ HQALVTLWHQ LHVDMKSLLA WQSLSRDIQL
1060 1070 1080 1090 1100
IRSWSLVTFR TLKPEEQRQA LRNLELHYQA FLRDSQDAGG FGPEDRLVAE
1110 1120 1130 1140 1150
REYGSCSRHY QQLLQSLEQG EQEESRCQRC ISELKDIRLQ LEACETRTVH
1160 1170 1180 1190 1200
RLRLPLDKDP ARECAQRIAE QQKAQAEVEG LGKGVARLSA EAEKVLALPE
1210 1220 1230 1240 1250
PSPAAPTLRS ELELTLGKLE QVRSLSAIYL EKLKTISLVI RSTQGAEEVL
1260 1270 1280 1290 1300
KTHEEQLKEA QAVPATLQEL EATKASLKKL RAQAEAQQPV FNTLRDELRG
1310 1320 1330 1340 1350
AQEVGERLQQ RHGERDVEVE RWRERVTQLL ERWQAVLAQT DVRQRELEQL
1360 1370 1380 1390 1400
GRQLRYYRES ADPLSAWLQD AKRRQEQIQA VPIANCQAAR EQLRQEKALL
1410 1420 1430 1440 1450
EEIERHGEKV EECQKFAKQY INAIKDYELQ LITYKAQLEP VASPAKKPKV
1460 1470 1480 1490 1500
QSGSESVIQE YVDLRTRYSE LTTLTSQYIK FISETLRRME EEERLAEQQR
1510 1520 1530 1540 1550
AEERERLAEV EAALEKQRQL AEAHAQAKAQ AELEAQELQR RMQEEVARRE
1560 1570 1580 1590 1600
EAAVDAQQQK RSIQEELQHL RQSSEAEIQA KAQQVEAAER SRMRIEEEIR
1610 1620 1630 1640 1650
VVRLQLETTE RQRGGAEGEL QALRARAEEA EAQKRQAQEE AERLRRQVQD
1660 1670 1680 1690 1700
ESQRKRQAEA ELALRVKAEA EAAREKQRAL QALDELRLQA EEAERRLRQA
1710 1720 1730 1740 1750
EAERARQVQV ALETAQRSAE VELQSKRASF AEKTAQLERT LQEEHVTVAQ
1760 1770 1780 1790 1800
LREEAERRAQ QQAEAERARE EAERELERWQ LKANEALRLR LQAEEVAQQK
1810 1820 1830 1840 1850
SLAQADAEKQ KEEAEREARR RGKAEEQAVR QRELAEQELE KQRQLAEGTA
1860 1870 1880 1890 1900
QQRLAAEQEL IRLRAETEQG EQQRQLLEEE LARLQHEATA ATQKRQELEA
1910 1920 1930 1940 1950
ELAKVRAEME VLLASKARAE EESRSTSEKS KQRLEAEAGR FRELAEEAAR
1960 1970 1980 1990 2000
LRALAEEAKR QRQLAEEDAA RQRAEAERVL TEKLAAISEA TRLKTEAEIA
2010 2020 2030 2040 2050
LKEKEAENER LRRLAEDEAF QRRRLEEQAA LHKADIEERL AQLRKASESE
2060 2070 2080 2090 2100
LERQKGLVED TLRQRRQVEE EIMALKVSFE KAAAGKAELE LELGRIRSNA
2110 2120 2130 2140 2150
EDTMRSKEQA ELEAARQRQL AAEEEQRRRE AEERVQRSLA AEEEAARQRK
2160 2170 2180 2190 2200
VALEEVERLK AKVEEARRLR ERAEQESARQ LQLAQEAAQK RLQAEEKAHA
2210 2220 2230 2240 2250
FVVQQREEEL QQTLQQEQNM LDRLRSEAEA ARRAAEEAEE AREQAEREAA
2260 2270 2280 2290 2300
QSRKQVEEAE RLKQSAEEQA QAQAQAQAAA EKLRKEAEQE AARRAQAEQA
2310 2320 2330 2340 2350
ALKQKQAADA EMEKHKKFAE QTLRQKAQVE QELTTLRLQL EETDHQKSIL
2360 2370 2380 2390 2400
DEELQRLKAE VTEAARQRSQ VEEELFSVRV QMEELGKLKA RIEAENRALI
2410 2420 2430 2440 2450
LRDKDNTQRF LEEEAEKMKQ VAEEAARLSV AAQEAARLRQ LAEEDLAQQR
2460 2470 2480 2490 2500
ALAEKMLKEK MQAVQEATRL KAEAELLQQQ KELAQEQARR LQEDKEQMAQ
2510 2520 2530 2540 2550
QLVEETQGFQ RTLEAERQRQ LEMSAEAERL KLRMAEMSRA QARAEEDAQR
2560 2570 2580 2590 2600
FRKQAEEIGE KLHRTELATQ EKVTLVQTLE IQRQQSDHDA ERLREAIAEL
2610 2620 2630 2640 2650
EREKEKLKQE AKLLQLKSEE MQTVQQEQIL QETQALQKSF LSEKDSLLQR
2660 2670 2680 2690 2700
ERFIEQEKAK LEQLFQDEVA KAKQLREEQQ RQQQQMEQEK QELMASMEEA
2710 2720 2730 2740 2750
RRRQREAEEG VRRKQEELQH LEQQRQQQEK LLAEENQRLR ERLQRLEEEH
2760 2770 2780 2790 2800
RAALAHSEIA TTQAASTKAL PNGRDAPDGP SVEAEPEYTF EGLRQKVPAQ
2810 2820 2830 2840 2850
QLQEAGILSQ EELQRLAQGH TTVAELTQRE DVYRYLKGRS SIAGLLLKPT
2860 2870 2880 2890 2900
NEKLSVYTAL QRQLLSPGTA LILLEAQAAS GFLLDPVRNR RLTVNEAVKE
2910 2920 2930 2940 2950
GVVGPELHHK LLSAERAVTG YKDPYTGEQI SLFQAMKKDL IVRDHGVRLL
2960 2970 2980 2990 3000
EAQIATGGII DPVHSHRVPV DVAYKRGYFD EEMNRILSDP SDDTKGFFDP
3010 3020 3030 3040 3050
NTHENLTYLQ LLERCVEDPE TGLRLLPLTD KAAKGGELVY TDTEARDVFE
3060 3070 3080 3090 3100
KATVSAPFGK FQGRTVTIWE IINSEYFTAE QRRDLLQQFR TGHITVEKII
3110 3120 3130 3140 3150
KIVITVVEEH ERKGQLCFEG LRALVPAAEL LDSGVISHEL YQQLQRGERS
3160 3170 3180 3190 3200
VREVAEADSV RQALRGTNVI AGVWLEEAGQ KLSIYEALKK DLLQPEVAVA
3210 3220 3230 3240 3250
LLEAQAGTGH IIDPATSARL TVDEAVRAGL VGPELHEKLL SAEKAVTGYR
3260 3270 3280 3290 3300
DPYSGQSVSL FQALKKGLIP REQGLRLLDA QLSTGGIVDP SKSHRVPLDV
3310 3320 3330 3340 3350
AYARGYLDKE TNRALTSPRD DARVYHDPST QEPVTYSQLQ QRCRSDQLTG
3360 3370 3380 3390 3400
LSLLPLSEKA VRARQEEVYS ELQARETLEQ AKVEVPVGSF KGRAMTVWEL
3410 3420 3430 3440 3450
ISSEYFTEEQ RQELLRQFRT GKVTVEKVIK IVITIVEEVE TRRQERLSFS
3460 3470 3480 3490 3500
GLRAPVPASE LLDAKILSRA QFDQLKDGKT SVKELSEVGS VRTLLQGSGC
3510 3520 3530 3540 3550
LAGIYLEDSK EKVTIYEAMR RGLLRPSTAT LLLEAQAATG FLVDPVRNQR
3560 3570 3580 3590 3600
LYVHEAVKAG VVGPELHEKL LSAEKAVTGY KDPYSGNTIS LFQAMKKGLV
3610 3620 3630 3640 3650
LRDHAIRLLE AQVATGGIID PVHSHRLPVD VAYQRGYFDE EMNRVLADPS
3660 3670 3680 3690 3700
DDTKGFFDPN THENLTYLQL LERCVEDPET GLRLLPLKGA EKTEVVETTQ
3710 3720 3730 3740 3750
VYTEEETRRA FEETQIDIPG GGSHGGSSMS LWEVMQSNMI PEDQRARLMA
3760 3770 3780 3790 3800
DFQAGRVTKE RMIIIIIEII EKTEIIRQQN LASYDYVRRR LTAEDLYEAR
3810 3820 3830 3840 3850
IISLETYNLF REGTKNLREV LEMESAWRYL YGTGAVAGVY LPGSRQTLTI
3860 3870 3880 3890 3900
YQALKKGLLS AEVARLLLEA QAATGFLLDP VKGERLTVDE AVRKGLVGPE
3910 3920 3930 3940 3950
LHDRLLSAER AVTGYRDPYT EQTISLFQAM KKELIPAEEA LRLLDAQLAT
3960 3970 3980 3990 4000
GGIVDPRLGF HLPLEVAYQR GYLNKDTHDQ LSEPSEVRSY VDPSTDERLS
4010 4020 4030 4040 4050
YTQLLKRCRR DDPSGQMLLL LSDARKLTFR GLRKQITVEE LVRSQVMDEA
4060 4070 4080 4090 4100
TALQLQEGLT SIEEVTKNLQ KFLEGTSCIA GVFVDATKER LSVYQAMKKG
4110 4120 4130 4140 4150
IIRPGTAFEL LEAQAATGYV IDPIKGLKLT VEEAVRMGIV GPEFKDKLLS
4160 4170 4180 4190 4200
AERAVTGYKD PYSGKLISLF QAMKKGLILK DHGIRLLEAQ IATGGIIDPE
4210 4220 4230 4240 4250
ESHRLPVEVA YKRGLFDEEM NEILTDPSDD TKGFFDPNTE ENLTYLQLME
4260 4270 4280 4290 4300
RCITDPQTGL CLLPLKEKKR ERKTSSKSSV RKRRVVIVDP ETGKEMSVYE
4310 4320 4330 4340 4350
AYRKGLIDHQ TYLELSEQEC EWEEITISSS DGVVKSMIID RRSGRQYDID
4360 4370 4380 4390 4400
DAITKNLIDR SALDQYRAGT LSITEFADML SGNAGGFRSR SSSVGSSSSY
4410 4420 4430 4440 4450
PISSAGPRTQ LASWSDPTEE TGPVAGILDT ETLEKVSITE AMHRNLVDNI
4460 4470 4480 4490 4500
TGQRLLEAQA CTGGIIDPST GERFPVTEAV NKGLVDKIMV DRINLAQKAF
4510 4520 4530 4540 4550
CGFEDPRTKT KMSAAQALKK GWLYYEAGQR FLEVQYLTGG LIEPDTPGRV
4560 4570 4580 4590 4600
SLDEALQRGT VDARTAQKLR DVSAYSKYLT CPKTKLKISY KDALDRSMVE
4610 4620 4630 4640 4650
EGTGLRLLEA AAQSSKGYYS PYSVSGSGST AGSRTGSRTG SRAGSRRGSF
4660 4670 4680 4690
DATGSGFSMT FSSSSYSSSG YGRRYASGPS ASLGGPESAV A
Length:4,691
Mass (Da):534,188
Last modified:April 16, 2014 - v3
Checksum:i91A09EC8181137D1
GO
Isoform PLEC-1 (identifier: Q9QXS1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     202-206: Missing.

Show »
Length:4,686
Mass (Da):533,508
Checksum:i286192092142820A
GO
Isoform PLEC-1A (identifier: Q9QXS1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH → MSQHRLRVPEPEGLGSKRTSSEDNLYLAVLRASEGKK
     38-180: Missing.
     202-206: Missing.

Show »
Length:4,543
Mass (Da):517,287
Checksum:i0DEF1312838F3117
GO
Isoform PLEC-1B,2A (identifier: Q9QXS1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH → MEPSGSLFPSLVVVGHVVTLAAVWHWRKGHRQAKDEQ
     38-180: Missing.

Show »
Length:4,548
Mass (Da):517,980
Checksum:i7E79CDB6FA6FA113
GO
Isoform PLEC-1B (identifier: Q9QXS1-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH → MEPSGSLFPSLVVVGHVVTLAAVWHWRKGHRQAKDEQ
     38-180: Missing.
     202-206: Missing.

Show »
Length:4,543
Mass (Da):517,300
Checksum:iC6F750A867F64F15
GO
Isoform PLEC-0,1C (identifier: Q9QXS1-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MVAGMLMPLD...ARGLVRETFA → MSGEDSEVRP...PAERAVIRIA
     67-180: Missing.
     202-206: Missing.

Show »
Length:4,572
Mass (Da):519,755
Checksum:i32917732E7F62B40
GO
Isoform PLEC-0,1C,2A (identifier: Q9QXS1-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MVAGMLMPLD...ARGLVRETFA → MSGEDSEVRP...PAERAVIRIA
     67-180: Missing.

Show »
Length:4,577
Mass (Da):520,435
Checksum:iB341CDEA4AEBC734
GO
Isoform PLEC-0,1C,2A,3A (identifier: Q9QXS1-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MVAGMLMPLD...ARGLVRETFA → MSGEDSEVRP...PAERAVIRIA
     67-180: Missing.
     239-239: E → ERDVIRSVRLPRE

Show »
Length:4,589
Mass (Da):521,913
Checksum:i16CAABE9A305F7A3
GO
Isoform PLEC-1D,2A (identifier: Q9QXS1-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MVAGM → MKIVP
     6-180: Missing.

Show »
Length:4,516
Mass (Da):514,413
Checksum:i36BEE7A763630B5D
GO
Isoform PLEC-1D (identifier: Q9QXS1-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MVAGM → MKIVP
     6-180: Missing.
     202-206: Missing.

Show »
Length:4,511
Mass (Da):513,733
Checksum:i9A5D1ED70F20893E
GO
Isoform PLEC-1E,2A (identifier: Q9QXS1-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MVAGMLMPLDRLRAI → MDPSRAIQHEISSLK
     16-180: Missing.

Show »
Length:4,526
Mass (Da):515,538
Checksum:i50629AD9DAD55935
GO
Isoform PLEC-1E (identifier: Q9QXS1-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MVAGMLMPLDRLRAI → MDPSRAIQHEISSLK
     16-180: Missing.
     202-206: Missing.

Show »
Length:4,521
Mass (Da):514,858
Checksum:iDC0F769A3EBA7CA3
GO
Isoform PLEC-1F (identifier: Q9QXS1-13) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: MVAGMLMPLDRLRAIYEVLFREGVMVAK → MAHLLTSGPPPDEQDFIQAYEEVREKYK
     29-180: Missing.
     202-206: Missing.

Show »
Length:4,534
Mass (Da):516,439
Checksum:i552158F027E35E2F
GO
Isoform PLEC-1G (identifier: Q9QXS1-14) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MVAGMLMPLD...SLHPHVPGVT → MAGTWAAKGV...GYLYGQLCCV
     45-180: Missing.
     202-206: Missing.

Show »
Length:4,550
Mass (Da):518,098
Checksum:iE3F452D98F8841B1
GO
Isoform PLEC-1H (identifier: Q9QXS1-15) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-242: Missing.

Show »
Length:4,449
Mass (Da):506,427
Checksum:iC1A063931DEE299C
GO
Isoform PLEC-1I (identifier: Q9QXS1-16) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRP → MNETVCRRKLSPSGSTNTLSRLRGTSVTCTKTS
     34-180: Missing.

Show »
Length:4,544
Mass (Da):517,399
Checksum:iCCE0F23C0BA8CD6D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2535 – 25351A → V in AAR95666 (PubMed:14672974).Curated
Sequence conflicti2535 – 25351A → V in AAR95671 (PubMed:14672974).Curated
Sequence conflicti2535 – 25351A → V in AAR95676 (PubMed:14672974).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 242242Missing in isoform PLEC-1H. CuratedVSP_005040Add
BLAST
Alternative sequencei1 – 6666MVAGM…RETFA → MSGEDSEVRPVAVAEGSSNG SSGSPSPGDTLPWNLGKTQR SRRSGGGSVGNGSVLDPAER AVIRIA in isoform PLEC-0,1C, isoform PLEC-0,1C,2A,3A and isoform PLEC-0,1C,2A. CuratedVSP_005039Add
BLAST
Alternative sequencei1 – 4444MVAGM…VPGVT → MAGTWAAKGVFTSQREVLLE RPCWLDGGCEQVRRGYLYGQ LCCV in isoform PLEC-1G. CuratedVSP_005038Add
BLAST
Alternative sequencei1 – 3737MVAGM…PRSLH → MSQHRLRVPEPEGLGSKRTS SEDNLYLAVLRASEGKK in isoform PLEC-1A. CuratedVSP_005036Add
BLAST
Alternative sequencei1 – 3737MVAGM…PRSLH → MEPSGSLFPSLVVVGHVVTL AAVWHWRKGHRQAKDEQ in isoform PLEC-1B and isoform PLEC-1B,2A. CuratedVSP_005037Add
BLAST
Alternative sequencei1 – 3333MVAGM…KDRRP → MNETVCRRKLSPSGSTNTLS RLRGTSVTCTKTS in isoform PLEC-1I. CuratedVSP_005035Add
BLAST
Alternative sequencei1 – 2828MVAGM…VMVAK → MAHLLTSGPPPDEQDFIQAY EEVREKYK in isoform PLEC-1F. CuratedVSP_005034Add
BLAST
Alternative sequencei1 – 1515MVAGM…RLRAI → MDPSRAIQHEISSLK in isoform PLEC-1E and isoform PLEC-1E,2A. CuratedVSP_005033Add
BLAST
Alternative sequencei1 – 55MVAGM → MKIVP in isoform PLEC-1D and isoform PLEC-1D,2A. CuratedVSP_005032
Alternative sequencei6 – 180175Missing in isoform PLEC-1D and isoform PLEC-1D,2A. CuratedVSP_005041Add
BLAST
Alternative sequencei16 – 180165Missing in isoform PLEC-1E and isoform PLEC-1E,2A. CuratedVSP_005042Add
BLAST
Alternative sequencei29 – 180152Missing in isoform PLEC-1F. CuratedVSP_005043Add
BLAST
Alternative sequencei34 – 180147Missing in isoform PLEC-1I. CuratedVSP_005044Add
BLAST
Alternative sequencei38 – 180143Missing in isoform PLEC-1A, isoform PLEC-1B and isoform PLEC-1B,2A. CuratedVSP_005045Add
BLAST
Alternative sequencei45 – 180136Missing in isoform PLEC-1G. CuratedVSP_005046Add
BLAST
Alternative sequencei67 – 180114Missing in isoform PLEC-0,1C, isoform PLEC-0,1C,2A and isoform PLEC-0,1C,2A,3A. CuratedVSP_005047Add
BLAST
Alternative sequencei202 – 2065Missing in isoform PLEC-1, isoform PLEC-1A, isoform PLEC-1B, isoform PLEC-1D, isoform PLEC-1E, isoform PLEC-1G, isoform PLEC-1F and isoform PLEC-0,1C. CuratedVSP_005048
Alternative sequencei239 – 2391E → ERDVIRSVRLPRE in isoform PLEC-0,1C,2A,3A. CuratedVSP_005049

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY480033 mRNA. Translation: AAR95666.1.
AY480038 mRNA. Translation: AAR95671.1.
AY480043 mRNA. Translation: AAR95676.1.
AC110211 Genomic DNA. No translation available.
AF188006 mRNA. Translation: AAF18066.1.
AF188007 mRNA. Translation: AAF18067.1.
AF188008 mRNA. Translation: AAF18068.1.
AF188009 mRNA. Translation: AAF18069.1.
AF188010 mRNA. Translation: AAF18070.1.
AF188011 mRNA. Translation: AAF18071.1.
AF188012 mRNA. Translation: AAF18072.1.
AF188013 mRNA. Translation: AAF18073.1.
AF188014 mRNA. Translation: AAF18074.1.
AF188015 mRNA. Translation: AAF18075.1.
AF188016 mRNA. Translation: AAF18076.1.
AF188017 mRNA. Translation: AAF18077.1.
AF188018 mRNA. Translation: AAF18078.1.
AF188019 mRNA. Translation: AAF18079.1.
AF188020 mRNA. Translation: AAF18080.1.
AF188021 mRNA. Translation: AAF18081.1.
AF188022 mRNA. Translation: AAF18082.1.
AF188023 mRNA. Translation: AAF18083.1.
AK017743 mRNA. No translation available.
CCDSiCCDS37113.1. [Q9QXS1-13]
CCDS37114.1. [Q9QXS1-2]
CCDS37115.1. [Q9QXS1-14]
CCDS37116.1. [Q9QXS1-3]
CCDS49644.1. [Q9QXS1-5]
CCDS49645.1. [Q9QXS1-4]
CCDS49646.1. [Q9QXS1-10]
CCDS49647.1. [Q9QXS1-1]
CCDS49648.1. [Q9QXS1-12]
CCDS49649.1. [Q9QXS1-8]
PIRiD59404.
RefSeqiNP_001157012.1. NM_001163540.1. [Q9QXS1-1]
NP_001157014.1. NM_001163542.1. [Q9QXS1-8]
NP_001157021.1. NM_001163549.1. [Q9QXS1-4]
NP_001157675.1. NM_001164203.1.
NP_035247.2. NM_011117.2. [Q9QXS1-6]
NP_958791.2. NM_201389.2. [Q9QXS1-2]
NP_958796.2. NM_201394.2. [Q9QXS1-3]
UniGeneiMm.234912.

Genome annotation databases

EnsembliENSMUST00000023226; ENSMUSP00000023226; ENSMUSG00000022565. [Q9QXS1-3]
ENSMUST00000054449; ENSMUSP00000057158; ENSMUSG00000022565. [Q9QXS1-4]
ENSMUST00000071869; ENSMUSP00000071765; ENSMUSG00000022565. [Q9QXS1-12]
ENSMUST00000072692; ENSMUSP00000072478; ENSMUSG00000022565. [Q9QXS1-14]
ENSMUST00000073418; ENSMUSP00000073124; ENSMUSG00000022565. [Q9QXS1-1]
ENSMUST00000074834; ENSMUSP00000074383; ENSMUSG00000022565. [Q9QXS1-13]
ENSMUST00000076442; ENSMUSP00000075772; ENSMUSG00000022565. [Q9QXS1-2]
ENSMUST00000089610; ENSMUSP00000087037; ENSMUSG00000022565. [Q9QXS1-8]
ENSMUST00000169108; ENSMUSP00000126068; ENSMUSG00000022565. [Q9QXS1-10]
ENSMUST00000169714; ENSMUSP00000126526; ENSMUSG00000022565. [Q9QXS1-5]
GeneIDi18810.
KEGGimmu:18810.
UCSCiuc007wir.2. mouse. [Q9QXS1-3]
uc007wis.2. mouse. [Q9QXS1-14]
uc007wit.2. mouse. [Q9QXS1-1]
uc007wiu.2. mouse. [Q9QXS1-5]
uc007wiv.2. mouse. [Q9QXS1-10]
uc007wiw.2. mouse. [Q9QXS1-2]
uc007wiz.2. mouse. [Q9QXS1-12]
uc007wja.2. mouse. [Q9QXS1-13]
uc007wjb.2. mouse. [Q9QXS1-6]
uc007wjd.2. mouse. [Q9QXS1-4]
uc011zuq.1. mouse. [Q9QXS1-8]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY480033 mRNA. Translation: AAR95666.1.
AY480038 mRNA. Translation: AAR95671.1.
AY480043 mRNA. Translation: AAR95676.1.
AC110211 Genomic DNA. No translation available.
AF188006 mRNA. Translation: AAF18066.1.
AF188007 mRNA. Translation: AAF18067.1.
AF188008 mRNA. Translation: AAF18068.1.
AF188009 mRNA. Translation: AAF18069.1.
AF188010 mRNA. Translation: AAF18070.1.
AF188011 mRNA. Translation: AAF18071.1.
AF188012 mRNA. Translation: AAF18072.1.
AF188013 mRNA. Translation: AAF18073.1.
AF188014 mRNA. Translation: AAF18074.1.
AF188015 mRNA. Translation: AAF18075.1.
AF188016 mRNA. Translation: AAF18076.1.
AF188017 mRNA. Translation: AAF18077.1.
AF188018 mRNA. Translation: AAF18078.1.
AF188019 mRNA. Translation: AAF18079.1.
AF188020 mRNA. Translation: AAF18080.1.
AF188021 mRNA. Translation: AAF18081.1.
AF188022 mRNA. Translation: AAF18082.1.
AF188023 mRNA. Translation: AAF18083.1.
AK017743 mRNA. No translation available.
CCDSiCCDS37113.1. [Q9QXS1-13]
CCDS37114.1. [Q9QXS1-2]
CCDS37115.1. [Q9QXS1-14]
CCDS37116.1. [Q9QXS1-3]
CCDS49644.1. [Q9QXS1-5]
CCDS49645.1. [Q9QXS1-4]
CCDS49646.1. [Q9QXS1-10]
CCDS49647.1. [Q9QXS1-1]
CCDS49648.1. [Q9QXS1-12]
CCDS49649.1. [Q9QXS1-8]
PIRiD59404.
RefSeqiNP_001157012.1. NM_001163540.1. [Q9QXS1-1]
NP_001157014.1. NM_001163542.1. [Q9QXS1-8]
NP_001157021.1. NM_001163549.1. [Q9QXS1-4]
NP_001157675.1. NM_001164203.1.
NP_035247.2. NM_011117.2. [Q9QXS1-6]
NP_958791.2. NM_201389.2. [Q9QXS1-2]
NP_958796.2. NM_201394.2. [Q9QXS1-3]
UniGeneiMm.234912.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SH5X-ray2.00A/B181-417[»]
1SH6X-ray2.00A181-417[»]
4Q57X-ray1.80B181-411[»]
ProteinModelPortaliQ9QXS1.
SMRiQ9QXS1. Positions 5-101, 181-411, 424-641, 661-1033, 3448-3688, 4028-4267, 4410-4613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202243. 11 interactions.
DIPiDIP-32004N.
IntActiQ9QXS1. 6 interactions.
MINTiMINT-1867366.
STRINGi10090.ENSMUSP00000073124.

PTM databases

iPTMnetiQ9QXS1.
PhosphoSiteiQ9QXS1.
SwissPalmiQ9QXS1.

Proteomic databases

EPDiQ9QXS1.
MaxQBiQ9QXS1.
PaxDbiQ9QXS1.
PeptideAtlasiQ9QXS1.
PRIDEiQ9QXS1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023226; ENSMUSP00000023226; ENSMUSG00000022565. [Q9QXS1-3]
ENSMUST00000054449; ENSMUSP00000057158; ENSMUSG00000022565. [Q9QXS1-4]
ENSMUST00000071869; ENSMUSP00000071765; ENSMUSG00000022565. [Q9QXS1-12]
ENSMUST00000072692; ENSMUSP00000072478; ENSMUSG00000022565. [Q9QXS1-14]
ENSMUST00000073418; ENSMUSP00000073124; ENSMUSG00000022565. [Q9QXS1-1]
ENSMUST00000074834; ENSMUSP00000074383; ENSMUSG00000022565. [Q9QXS1-13]
ENSMUST00000076442; ENSMUSP00000075772; ENSMUSG00000022565. [Q9QXS1-2]
ENSMUST00000089610; ENSMUSP00000087037; ENSMUSG00000022565. [Q9QXS1-8]
ENSMUST00000169108; ENSMUSP00000126068; ENSMUSG00000022565. [Q9QXS1-10]
ENSMUST00000169714; ENSMUSP00000126526; ENSMUSG00000022565. [Q9QXS1-5]
GeneIDi18810.
KEGGimmu:18810.
UCSCiuc007wir.2. mouse. [Q9QXS1-3]
uc007wis.2. mouse. [Q9QXS1-14]
uc007wit.2. mouse. [Q9QXS1-1]
uc007wiu.2. mouse. [Q9QXS1-5]
uc007wiv.2. mouse. [Q9QXS1-10]
uc007wiw.2. mouse. [Q9QXS1-2]
uc007wiz.2. mouse. [Q9QXS1-12]
uc007wja.2. mouse. [Q9QXS1-13]
uc007wjb.2. mouse. [Q9QXS1-6]
uc007wjd.2. mouse. [Q9QXS1-4]
uc011zuq.1. mouse. [Q9QXS1-8]

Organism-specific databases

CTDi5339.
MGIiMGI:1277961. Plec.

Phylogenomic databases

eggNOGiKOG0516. Eukaryota.
KOG3344. Eukaryota.
COG5045. LUCA.
COG5069. LUCA.
GeneTreeiENSGT00760000119163.
HOVERGENiHBG053616.
InParanoidiQ9QXS1.
KOiK10388.
OMAiYLNKDTH.

Enzyme and pathway databases

ReactomeiR-MMU-2022090. Assembly of collagen fibrils and other multimeric structures.
R-MMU-264870. Caspase-mediated cleavage of cytoskeletal proteins.
R-MMU-446107. Type I hemidesmosome assembly.

Miscellaneous databases

EvolutionaryTraceiQ9QXS1.
PROiQ9QXS1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXS1.
CleanExiMM_PLEC1.
ExpressionAtlasiQ9QXS1. baseline and differential.
GenevisibleiQ9QXS1. MM.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
3.90.1290.10. 7 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR030269. Plectin.
IPR001101. Plectin_repeat.
IPR005326. S10_plectin_N.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PANTHERiPTHR11915:SF247. PTHR11915:SF247. 4 hits.
PfamiPF00307. CH. 2 hits.
PF00681. Plectin. 18 hits.
PF03501. S10_plectin. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00250. PLEC. 35 hits.
SM00150. SPEC. 6 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF75399. SSF75399. 8 hits.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Unusual 5' transcript complexity of plectin isoforms: novel tissue-specific exons modulate actin binding activity."
    Fuchs P., Zoerer M., Rezniczek G.A., Spazierer D., Oehler S., Castanon M.J., Hauptmann R., Wiche G.
    Hum. Mol. Genet. 8:2461-2472(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-964, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Brain, Embryo, Heart, Kidney, Skeletal muscle and Testis.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-812.
    Strain: C57BL/6J.
    Tissue: Embryo.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 629-633, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "Direct binding of plectin to Fer kinase and negative regulation of its catalytic activity."
    Lunter P.C., Wiche G.
    Biochem. Biophys. Res. Commun. 296:904-910(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FER.
  7. "Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin."
    Wilhelmsen K., Litjens S.H.M., Kuikman I., Tshimbalanga N., Janssen H., van den Bout I., Raymond K., Sonnenberg A.
    J. Cell Biol. 171:799-810(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYNE3.
  8. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2788; TYR-3040; TYR-3369; TYR-3797 AND TYR-4622, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26 (ISOFORM PLEC-1A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  11. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  12. "Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
    Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
    Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-823, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
    Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
    J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOR1A.
  15. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4393 AND SER-4396, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM PLEC-1A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4389 AND SER-4393, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM PLEC-1A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728; SER-1055; THR-4037; SER-4389; SER-4391; SER-4392; SER-4393; SER-4396; SER-4620; SER-4625; SER-4629; THR-4630; SER-4633 AND SER-4649, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 (ISOFORM PLEC-1A), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  19. "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
    Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
    Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DST.
  20. "Periaxin is required for hexagonal geometry and membrane organization of mature lens fibers."
    Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J., Rao P.V.
    Dev. Biol. 357:179-190(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK; BFSP1; BFSP2; ANK2; PRX; VIM AND SPECTRIN.
  21. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1733; LYS-2644 AND LYS-3060, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  22. "Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin."
    Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G.
    Eur. J. Biochem. 271:1873-1884(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 181-417, INTERACTION WITH VIM.

Entry informationi

Entry nameiPLEC_MOUSE
AccessioniPrimary (citable) accession number: Q9QXS1
Secondary accession number(s): E9QN87
, Q6S384, Q6S389, Q6S394, Q9CS65, Q9QUT2, Q9QXQ8, Q9QXQ9, Q9QXR0, Q9QXR1, Q9QXR2, Q9QXR3, Q9QXR4, Q9QXR5, Q9QXR6, Q9QXR7, Q9QXR8, Q9QXR9, Q9QXS0, Q9QXS2, Q9QXS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: April 16, 2014
Last modified: July 6, 2016
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.