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E9Q557

- DESP_MOUSE

UniProt

E9Q557 - DESP_MOUSE

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Protein

Desmoplakin

Gene

Dsp

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

Functioni

Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin-plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes.

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
  2. structural molecule activity Source: Ensembl

GO - Biological processi

  1. adherens junction organization Source: MGI
  2. bundle of His cell to Purkinje myocyte communication Source: Ensembl
  3. desmosome organization Source: BHF-UCL
  4. intermediate filament cytoskeleton organization Source: MGI
  5. intermediate filament organization Source: BHF-UCL
  6. keratinocyte differentiation Source: Ensembl
  7. peptide cross-linking Source: Ensembl
  8. protein localization to adherens junction Source: BHF-UCL
  9. regulation of heart rate by cardiac conduction Source: Ensembl
  10. single organismal cell-cell adhesion Source: MGI
  11. skin development Source: MGI
  12. ventricular cardiac muscle cell action potential Source: Ensembl
  13. ventricular compact myocardium morphogenesis Source: BHF-UCL
  14. wound healing Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Desmoplakin
Short name:
DP
Gene namesi
Name:Dsp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:109611. Dsp.

Subcellular locationi

Cell junctiondesmosome By similarity. Cytoplasmcytoskeleton By similarity
Note: Innermost portion of the desmosomal plaque. Colocalizes with epidermal KRT5-KRT14 and simple KRT8-KRT18 keratins and VIM intermediate filaments network (By similarity).By similarity

GO - Cellular componenti

  1. basolateral plasma membrane Source: MGI
  2. cell-cell junction Source: MGI
  3. cornified envelope Source: Ensembl
  4. desmosome Source: MGI
  5. extracellular vesicular exosome Source: Ensembl
  6. fascia adherens Source: Ensembl
  7. intercalated disc Source: MGI
  8. membrane Source: MGI
  9. mitochondrion Source: MGI
  10. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Keywords - Diseasei

Cardiomyopathy

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 28832883DesmoplakinPRO_0000410831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei178 – 1781PhosphoserineBy similarity
Modified residuei188 – 1881PhosphoserineBy similarity
Modified residuei2036 – 20361PhosphoserineBy similarity
Modified residuei2219 – 22191PhosphoserineBy similarity
Modified residuei2221 – 22211PhosphoserineBy similarity
Lipidationi2492 – 24921Omega-hydroxyceramide glutamate esterBy similarity
Modified residuei2827 – 28271PhosphoserineBy similarity
Modified residuei2832 – 28321PhosphoserineBy similarity
Modified residuei2836 – 28361Phosphoserine1 Publication
Modified residuei2860 – 28601PhosphoserineBy similarity
Modified residuei2864 – 28641PhosphothreonineBy similarity
Modified residuei2879 – 28791PhosphoserineBy similarity

Post-translational modificationi

Ser-2860 is probably phosphorylated by a cAMP-dependent protein kinase. Phosphorylation on Ser-2860 probably affects its association with epidermal, simple cytokeratins and VIM intermediate filaments (By similarity).By similarity
Substrate of transglutaminase. Some glutamines and lysines are cross-linked to other desmoplakin molecules, to other proteins such as keratin, envoplakin, periplakin and involucrin, and to lipids like omega-hydroxyceramide (By similarity).By similarity

Keywords - PTMi

Lipoprotein, Phosphoprotein

Proteomic databases

MaxQBiE9Q557.
PRIDEiE9Q557.

Expressioni

Gene expression databases

BgeeiE9Q557.
ExpressionAtlasiE9Q557. baseline and differential.

Interactioni

Subunit structurei

Homodimer. Interacts with COL17A1 (via cytoplasmic region). Associates (via C-terminal) with KRT5-KRT14 (via rod region), KRT8-KRT18 and VIM intermediate filaments. Interacts with PKP2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi224908. 3 interactions.
IntActiE9Q557. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliE9Q557.
SMRiE9Q557. Positions 190-639, 2221-2460, 2625-2820.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati190 – 28394Spectrin 1Add
BLAST
Repeati284 – 387104Spectrin 2Add
BLAST
Repeati388 – 45871Spectrin 3aAdd
BLAST
Domaini459 – 52769SH3Add
BLAST
Repeati528 – 55730Spectrin 3bAdd
BLAST
Repeati558 – 63982Spectrin 4Add
BLAST
Repeati666 – 781116Spectrin 5Add
BLAST
Repeati782 – 895114Spectrin 6Add
BLAST
Repeati2021 – 205737Plectin 1Add
BLAST
Repeati2058 – 209538Plectin 2Add
BLAST
Repeati2096 – 213338Plectin 3Add
BLAST
Repeati2134 – 217138Plectin 4Add
BLAST
Repeati2175 – 220935Plectin 5Add
BLAST
Repeati2210 – 224536Plectin 6Add
BLAST
Repeati2263 – 230038Plectin 7Add
BLAST
Repeati2301 – 233838Plectin 8Add
BLAST
Repeati2339 – 237638Plectin 9Add
BLAST
Repeati2377 – 241438Plectin 10Add
BLAST
Repeati2418 – 245235Plectin 11Add
BLAST
Repeati2468 – 250538Plectin 12Add
BLAST
Repeati2519 – 255638Plectin 13Add
BLAST
Repeati2622 – 265938Plectin 14Add
BLAST
Repeati2660 – 269738Plectin 15Add
BLAST
Repeati2736 – 277338Plectin 16Add
BLAST
Repeati2774 – 281138Plectin 17Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 10681068Globular 1Add
BLAST
Regioni1 – 596596Interacts with plakophilin 1 and junction plakoglobinBy similarityAdd
BLAST
Regioni1069 – 1957889Central fibrous rod domainAdd
BLAST
Regioni1958 – 2882925Globular 2Add
BLAST
Regioni1972 – 22202494.5 X 38 AA tandem repeats (Domain A)Add
BLAST
Regioni2256 – 24582034.5 X 38 AA tandem repeats (Domain B)Add
BLAST
Regioni2621 – 28332134.5 X 38 AA tandem repeats (Domain C)Add
BLAST
Regioni2835 – 2858246 X 4 AA tandem repeats of G-S-R-[SR]Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1034 – 1956923Sequence AnalysisAdd
BLAST

Domaini

Its association with epidermal and simple keratins is dependent on the tertiary structure induced by heterodimerization of these intermediate filaments proteins and most likely involves recognition sites located in the rod domain of these keratins.By similarity
The N-terminal region is required for localization to the desmosomal plaque and interacts with the N-terminal region of plakophilin 1.By similarity
The three tandem plakin repeat regions in the C-terminus mediate binding to intermediate filaments.By similarity

Sequence similaritiesi

Belongs to the plakin or cytolinker family.Curated
Contains 17 plectin repeats.Curated
Contains 1 SH3 domain.Curated
Contains 6 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00760000119163.
InParanoidiE9Q557.
KOiK10381.
OMAiKRSMSFQ.
TreeFamiTF106435.

Family and domain databases

Gene3Di3.90.1290.10. 4 hits.
InterProiIPR028462. Desmoplakin.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]
PANTHERiPTHR11915:SF234. PTHR11915:SF234. 1 hit.
PfamiPF00681. Plectin. 8 hits.
[Graphical view]
SMARTiSM00250. PLEC. 18 hits.
SM00150. SPEC. 2 hits.
[Graphical view]
SUPFAMiSSF75399. SSF75399. 5 hits.

Sequencei

Sequence statusi: Complete.

E9Q557 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSCNGGSHPR INTLGRMTRA ESGPDLRYEM TYSGGGGGGG GGGGGGTSRT
60 70 80 90 100
FYSHSRRCTV NDQNSDGYCQ TGTMSRHQNQ NTIQEMLQNC SDCLMRAELI
110 120 130 140 150
AQPELKFGEG MQLAWNRELD EYFTQANDQM EIIDGLIREM RQMGQPCDAY
160 170 180 190 200
QKRLLQLQEQ MRALYKAISV PRVRRASSKG AGGYTCQSGS GWDEFTKRLT
210 220 230 240 250
GECLGWMRQQ REEMDLMAWG VDAGSVEQHI NSHRSIHNTI GDYRWQLDKI
260 270 280 290 300
KADLREKSAI YQLEEEYENL LKASFERMDH LRQLQNIIQA TSREIMWIND
310 320 330 340 350
CEEEELLYDW SDKNTNIAQK QEAFSIRMSQ LEVKEKELNK LKQESDQLVL
360 370 380 390 400
NQHPASDKIE AYMDTLQTQW SWILQITKCI DVHLKENAAY FQFFEEAQST
410 420 430 440 450
EAYLKGLQDS IRKKYPCDKN MPLQHLLEQI KELEKEREKI IEYKRQVQNL
460 470 480 490 500
VNKSKKIVQL KPRNPDYRSN KPIILRALCD YKQDQKIVHK GDECILKDNN
510 520 530 540 550
ERSKWYVTGP GGVDMLVPSV GLIIPPPNPL AVDLSCKIEQ YYEAILALWN
560 570 580 590 600
QLYINMKSLV SWHYCMIDIE KIRAMTIAKL KTMRQEDYMK TIEDLELHYQ
610 620 630 640 650
DFIKNSQGSE MFGDDDKRRM QSQFTDAQKH YQTLVIQLPG HPQHQTVTKT
660 670 680 690 700
EITHLGTCQD VNHNKVIETN RENDKQETWL LMELQKIRRQ MEHCEARMTL
710 720 730 740 750
KNLLLAEQGS THHITVKINE LKSVQNDSQA LAEVLNQLKD MLANFRGSEK
760 770 780 790 800
YCYLQNEIFG LFQKLENING VSDGYLNSLC SVRALLQAIL QTEDMLKVYE
810 820 830 840 850
ARLTEEETVC LDLDKVEAYR CGLKKIKNDL NLKKSLLATM KTELQKAQQI
860 870 880 890 900
HSQSSQQYPL YDLDLGKFTE KVTQLTDRWQ KIDKQIDFRL WDLEKQIKQL
910 920 930 940 950
RNYRDNYQSF CKWLYDAKRR QDSLESMKFG DSNTVMRFLN EQKNLHSEIS
960 970 980 990 1000
GKRDKSEEVH KIAELCANSI KDYELQLASY TSGLETLLNI PIKRTMVQSP
1010 1020 1030 1040 1050
SGVILQEAAD IHARYIELLT RSGDYYRFLS EMLKSLEDLK LKNTKIEVLE
1060 1070 1080 1090 1100
EELRLARDAN SENCNKNKFL DQNLQKYQAE CSQFKAKLVS LEELKRQAEL
1110 1120 1130 1140 1150
DGKSAKQNLD KCYGQIKELN EKITRLTYEI EDEKRRRKTV EDRFDQQKND
1160 1170 1180 1190 1200
YDQLQKARQC EKENLSWQKL ESEKAIKEKE YEIERLRVLL QEEGARKREY
1210 1220 1230 1240 1250
ENELAKVRNH YNEEMSNLRN KYETEINITK TTIKEISMQK EDDSKNLRNQ
1260 1270 1280 1290 1300
MDRLSRENRD LKDEIVRLND SILQATEQRR RAEENALQQK ACGSETMQKK
1310 1320 1330 1340 1350
QRLEIELKQV IQQRSEDNAR HKQSLEEAAK TIQDKNKEIE RLKAEYQEEA
1360 1370 1380 1390 1400
KRRWEYENEL SKVRNSYDEE IISLKNQFET EINITKTTIH QLTMQKEEDT
1410 1420 1430 1440 1450
SGYRAQIDNL TRENRSLCEE VKRLKNTLAQ TTENLRRVEE NAQQQKATGS
1460 1470 1480 1490 1500
EMSQRKQQLE IELRQVTQMR TEESMRYKQS LDDAAKTIQD KNKEIERLKQ
1510 1520 1530 1540 1550
LVDKETNERK CLEDENSKLQ RVQYDLQKAN NSATEAMSKL KVQEQELTRL
1560 1570 1580 1590 1600
RIDYERVSQE RTVKDQDITR IQSSLKDLQL QKQKAEEELS RLKRTASDES
1610 1620 1630 1640 1650
SKRKMLEEEL EAMRRSLKEQ AVKITNLTQQ LEQASIVKKR SEDDLRQQRD
1660 1670 1680 1690 1700
VLDGHVREKQ RTQEELRRLS LDVEALRRQL VQEQENVKQA HLRNEHFQKA
1710 1720 1730 1740 1750
IEDKSRSLNE SKIEIERLQS LTENLTKEHL MLEEELRNLR LEYDDLRRGR
1760 1770 1780 1790 1800
SEADSDKNST ISELRSQLQI SNNRTLELQG LINDLQRERE NLRQEIEKFQ
1810 1820 1830 1840 1850
KQALEASNRI QESKSQCTQV VQERESLLVK IKVLEQDKAR LQRLEDELNR
1860 1870 1880 1890 1900
AKATLEAESR VKQRLECEKQ QIQNDLNQWK TQYSRKEETI RKIESEREKS
1910 1920 1930 1940 1950
EREKNSLRSE IERLQAEIKR IEERCRRKLE DSSRETQSQL ESERCRLQKE
1960 1970 1980 1990 2000
IEKLRQRPYG SHRETQTEYE WTVDSSKLVF DGLRKKVTAM QLYECQLIDK
2010 2020 2030 2040 2050
TTLDKLLKGK KSVEEVASEI QPFLRGAGAI AGASASPKEK YSLVEAKRKK
2060 2070 2080 2090 2100
FITPESTVML LEAQAATGGI IDPHRNEKLT VDNAVARDLI DFDDRQQIYT
2110 2120 2130 2140 2150
AEKAITGFDD PFSGKTVSVS EAIKKNLIDR ETGMRLLEAQ LASGGVVDPV
2160 2170 2180 2190 2200
NSVFLPKDVA LARGLIDRDL YRSLNDPRDS QKNFVDPITK KKVSYMQLRE
2210 2220 2230 2240 2250
RCRIEPHTGL LLLSVQKRSM SFQGIRQPVT VTELVDSGIL RPSTVNELES
2260 2270 2280 2290 2300
GQISYDEVGE RIKDFLQGSS CIAGIYNETT KQKLGIYEAM KIGLVRPGTA
2310 2320 2330 2340 2350
LELLEAQAAT GFIVDPVSNL RLPVEEAYKR GLVGIEFKEK LLSAERAVTG
2360 2370 2380 2390 2400
YNDPETGNII SLFQAMNKEL IEKGHGIRLL EAQIATGGII DPKESHRLPV
2410 2420 2430 2440 2450
DMAYKRGYFN EELSEILSDP SDDTKGFFDP NTEENLTYLQ LKERCIKDEE
2460 2470 2480 2490 2500
TGLCLLPLKE KKKQVQTSQK NTLRKRRVVI VDPETNKEMS VQEAYKKGLI
2510 2520 2530 2540 2550
DYDTFKELCE QECEWEEITI TGSDGSTRVV LVDRKTGSQY DIQDAIDKGL
2560 2570 2580 2590 2600
VDRKFFDQYR SGSLSLTQFA DMISLKNGVG NSSGLGGSVN DDVFSSSRHD
2610 2620 2630 2640 2650
SVSKISTISS VRNLTIRSSS LSDPLEESSP IAAIFDTENL EKISIAEGIE
2660 2670 2680 2690 2700
RGIVDSITGQ RLLEAQACTG GIIHPTTGQK LSLQDAVNQG LIDQDMATRL
2710 2720 2730 2740 2750
KPAQKAFIGF EGVKGKKKMS AAEAVKEKWL PYEAGQRFLE FQFLTGGLVD
2760 2770 2780 2790 2800
PEVHGRISTE EAIRKGFIDG RAAQRLQDIS SYAKILTCPK TKLKISYKDA
2810 2820 2830 2840 2850
MNRSMVEDIT GLRLLEAASV SSKGLPSPYN MSAPGSRSGS RSGSRSGSRS
2860 2870 2880
GSRSGSRRGS FDATGNSSYS YSYSFSSSSI GGY
Length:2,883
Mass (Da):332,912
Last modified:April 5, 2011 - v1
Checksum:i1D8B68788D519940
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC140331 Genomic DNA. No translation available.
CCDSiCCDS49239.1.
RefSeqiNP_076331.2. NM_023842.2.
UniGeneiMm.355327.

Genome annotation databases

EnsembliENSMUST00000124830; ENSMUSP00000115062; ENSMUSG00000054889.
GeneIDi109620.
KEGGimmu:109620.
UCSCiuc007qdk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC140331 Genomic DNA. No translation available.
CCDSi CCDS49239.1.
RefSeqi NP_076331.2. NM_023842.2.
UniGenei Mm.355327.

3D structure databases

ProteinModelPortali E9Q557.
SMRi E9Q557. Positions 190-639, 2221-2460, 2625-2820.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 224908. 3 interactions.
IntActi E9Q557. 4 interactions.

Proteomic databases

MaxQBi E9Q557.
PRIDEi E9Q557.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000124830 ; ENSMUSP00000115062 ; ENSMUSG00000054889 .
GeneIDi 109620.
KEGGi mmu:109620.
UCSCi uc007qdk.2. mouse.

Organism-specific databases

CTDi 1832.
MGIi MGI:109611. Dsp.

Phylogenomic databases

GeneTreei ENSGT00760000119163.
InParanoidi E9Q557.
KOi K10381.
OMAi KRSMSFQ.
TreeFami TF106435.

Miscellaneous databases

ChiTaRSi DSP. mouse.
NextBioi 362451.
PROi E9Q557.
SOURCEi Search...

Gene expression databases

Bgeei E9Q557.
ExpressionAtlasi E9Q557. baseline and differential.

Family and domain databases

Gene3Di 3.90.1290.10. 4 hits.
InterProi IPR028462. Desmoplakin.
IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
[Graphical view ]
PANTHERi PTHR11915:SF234. PTHR11915:SF234. 1 hit.
Pfami PF00681. Plectin. 8 hits.
[Graphical view ]
SMARTi SM00250. PLEC. 18 hits.
SM00150. SPEC. 2 hits.
[Graphical view ]
SUPFAMi SSF75399. SSF75399. 5 hits.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDESP_MOUSE
AccessioniPrimary (citable) accession number: E9Q557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: April 5, 2011
Last modified: October 29, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3