P15924 (DESP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Desmoplakin
Short name=DP

Alternative name(s):
250/210 kDa paraneoplastic pemphigus antigen

Gene names

Name:

DSP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2871 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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 DSC2. Ref.12 Ref.28
Subcellular location	Cell junction › desmosome. Cytoplasm › cytoskeleton. Note: Innermost portion of the desmosomal plaque. Colocalizes with epidermal KRT5-KRT14 and simple KRT8-KRT18 keratins and VIM intermediate filaments network. Ref.13
Tissue specificity	Isoform DPI is apparently an obligate constituent of all desmosomes. Isoform DPII resides predominantly in tissues and cells of stratified origin.
Domain	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. The N-terminal region is required for localization to the desmosomal plaque and interacts with the N-terminal region of plakophilin 1. The C-terminal region interacts with intermediate filaments.
Post-translational modification	Ser-2849 is probably phosphorylated by a cAMP-dependent protein kinase. Phosphorylation on Ser-2849 probably affects its association with epidermal, simple cytokeratins and VIM intermediate filaments. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 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.
Involvement in disease	Defects in DSP are the cause of palmoplantar keratoderma striate type 2 (SPPK2) [MIM:612908]; also known as keratosis palmoplantaris striata II. SPPK2 is characterized by skin thickening in the palms (linear pattern) and the soles (island-like pattern) and flexor aspect of the fingers. Abnormalities of the nails, the teeth and the hair are rarely present. Ref.9 Defects in DSP are the cause of cardiomyopathy dilated with woolly hair and keratoderma (DCWHK) [MIM:605676]; also known as Carvajal syndrome or palmoplantar keratoderma with left ventricular cardiomyopathy and woolly hair. DCWHK is an autosomal recessive cardiocutaneous syndrome characterized by a generalized striate keratoderma particularly affecting the palmoplantar epidermis, woolly hair, and dilated left ventricular cardiomyopathy. Ref.11 Defects in DSP are the cause of familial arrhythmogenic right ventricular dysplasia type 8 (ARVD8) [MIM:607450]; also known as arrhythmogenic right ventricular cardiomyopathy 8 (ARVC8). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall. Ref.29 Ref.33 Ref.34 Defects in DSP are the cause of skin fragility-woolly hair syndrome (SFWHS) [MIM:607655]. SFWHS is an autosomal recessive genodermatosis characterized by focal and diffuse palmoplantar keratoderma, hyperkeratotic plaques on the trunk and limbs, and woolly hair with varying degrees of alopecia. Ref.30 Defects in DSP are the cause of epidermolysis bullosa lethal acantholytic (EBLA) [MIM:609638]. EBLA is characterized by severe fragility of skin and mucous membranes. The phenotype is lethal in the neonatal period because of immense transcutaneous fluid loss. Typical features include universal alopecia, neonatal teeth, and nail loss. Histopathology of the skin shows suprabasal clefting and acantholysis throughout the spinous layer, mimicking pemphigus.
Sequence similarities	Belongs to the plakin or cytolinker family. Contains 17 plectin repeats. Contains 2 spectrin repeats.

Ontologies

Keywords
Cellular component	Cell junction Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cardiomyopathy Disease mutation Epidermolysis bullosa Palmoplantar keratoderma
Domain	Coiled coil Repeat
PTM	Lipoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular component disassembly involved in apoptosis Traceable author statement. Source: Reactome keratinocyte differentiation Inferred from direct assay. Source: UniProtKB peptide cross-linking Inferred from direct assay. Source: UniProtKB
Cellular component	cornified envelope Inferred from direct assay. Source: UniProtKB desmosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding, bridging Inferred from direct assay. Source: UniProtKB structural constituent of cytoskeleton Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform DPI (identifier: P15924-1)

Also known as: DP1;

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 DPII (identifier: P15924-2)

Also known as: DP2;

The sequence of this isoform differs from the canonical sequence as follows:
     1195-1793: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2871

2871

Desmoplakin

PRO_0000078144

Regions

Repeat

347 – 447

101

Spectrin 1

Repeat

858 – 952

95

Spectrin 2

Repeat

2009 – 2045

37

Plectin 1

Repeat

2046 – 2083

38

Plectin 2

Repeat

2084 – 2121

38

Plectin 3

Repeat

2122 – 2159

38

Plectin 4

Repeat

2163 – 2197

35

Plectin 5

Repeat

2198 – 2233

36

Plectin 6

Repeat

2251 – 2288

38

Plectin 7

Repeat

2289 – 2326

38

Plectin 8

Repeat

2327 – 2364

38

Plectin 9

Repeat

2365 – 2402

38

Plectin 10

Repeat

2406 – 2440

35

Plectin 11

Repeat

2456 – 2493

38

Plectin 12

Repeat

2507 – 2544

38

Plectin 13

Repeat

2610 – 2647

38

Plectin 14

Repeat

2648 – 2685

38

Plectin 15

Repeat

2724 – 2761

38

Plectin 16

Repeat

2762 – 2799

38

Plectin 17

Region

1 – 1056

1056

Globular 1

Region

1 – 584

584

Interacts with plakophilin 1 and junction plakoglobin

Region

1057 – 1945

889

Central fibrous rod domain

Region

1946 – 2871

926

Globular 2

Region

2824 – 2847

24

6 X 4 AA tandem repeats of G-S-R-[SR]

Coiled coil

1018 – 1945

928

Potential

Amino acid modifications

Modified residue

22

1

Phosphoserine Ref.15 Ref.19 Ref.23

Modified residue

28

1

Phosphotyrosine Ref.16 Ref.18

Modified residue

56

1

Phosphotyrosine Ref.16 Ref.18 Ref.25

Modified residue

165

1

Phosphoserine Ref.23

Modified residue

166

1

Phosphoserine Ref.23

Modified residue

176

1

Phosphoserine Ref.14 Ref.15 Ref.23

Modified residue

178

1

Phosphoserine Ref.24

Modified residue

1220

1

Phosphothreonine Ref.17

Modified residue

1225

1

Phosphoserine Ref.17

Modified residue

2024

1

Phosphoserine Ref.14 Ref.23

Modified residue

2209

1

Phosphoserine Ref.14 Ref.19 Ref.22 Ref.23

Modified residue

2275

1

Phosphotyrosine Ref.16

Modified residue

2606

1

Phosphoserine Ref.26

Modified residue

2815

1

Phosphoserine Ref.14 Ref.15 Ref.21 Ref.23

Modified residue

2820

1

Phosphoserine Ref.15 Ref.23

Modified residue

2821

1

Phosphoserine Ref.20 Ref.23

Modified residue

2825

1

Phosphoserine Ref.14 Ref.15 Ref.21 Ref.23

Modified residue

2849

1

Phosphoserine Ref.23

Modified residue

2853

1

Phosphothreonine Ref.23

Modified residue

2857

1

Phosphoserine Ref.23

Modified residue

2868

1

Phosphoserine Ref.23

Lipidation

2480

1

Omega-hydroxyceramide glutamate ester Potential

Natural variations

Alternative sequence

1195 – 1793

599

Missing in isoform DPII.

VSP_005070

Natural variant

287

1

N → K in SFWHS. Ref.30

VAR_015569

Natural variant

299

1

S → R in ARVD8. Ref.29 Ref.33 Ref.34

VAR_015402

Natural variant

305

1

I → F. Ref.34 Ref.35
Corresponds to variant rs17604693 [ dbSNP | Ensembl ].

VAR_033862

Natural variant

445

1

I → V in ARVD8.

VAR_065693

Natural variant

1255

1

R → K in ARVD8. Ref.33 Ref.34

VAR_023814

Natural variant

1505

1

A → V. Ref.34

VAR_065694

Natural variant

1512

1

Y → C. Ref.34 Ref.35
Corresponds to variant rs2076299 [ dbSNP | Ensembl ].

VAR_020468

Natural variant

1526

1

N → K. Ref.34 Ref.35

VAR_065695

Natural variant

1537

1

R → C. Ref.34 Ref.35

VAR_065696

Natural variant

1738

1

R → Q. Ref.34 Ref.35
Corresponds to variant rs6929069 [ dbSNP | Ensembl ].

VAR_023815

Natural variant

1775

1

R → I in ARVD8. Ref.33 Ref.34
Corresponds to variant rs34738426 [ dbSNP | Ensembl ].

VAR_023816

Natural variant

1833

1

E → V. Ref.28 Ref.35

VAR_065697

Natural variant

2366

1

R → C in SFWHS. Ref.30
Corresponds to variant rs28931610 [ dbSNP | Ensembl ].

VAR_015570

Natural variant

2375

1

G → R in a case of recessive arrhythmogenic right ventricular cardiomyopathy with skin abnormalities and woolly hair. Ref.31

VAR_018158

Experimental info

Mutagenesis

2849

1

S → G: Increases association with KRT5-KRT14, KRT8-KRT18 or VIM intermediate filaments. Ref.13

Sequence conflict

905

1

A → R in AAA85135. Ref.1

Sequence conflict

1120

1

D → R in AAA35766. Ref.4

Sequence conflict

2687 – 2688

2

RL → SV in AAA85135. Ref.1

Sequence conflict

2687 – 2688

2

RL → SV in AAA35766. Ref.4

Secondary structure

1

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2871

Helix Strand Turn

Details...

Beta strand

2213 – 2217

5

Helix

2219 – 2224

6

Helix

2230 – 2237

8

Helix

2246 – 2249

4

Helix

2251 – 2254

4

Beta strand

2260 – 2265

6

Turn

2266 – 2269

4

Beta strand

2270 – 2273

4

Helix

2274 – 2278

5

Beta strand

2279 – 2283

5

Helix

2285 – 2296

12

Beta strand

2301 – 2303

3

Turn

2304 – 2307

4

Beta strand

2308 – 2310

3

Helix

2312 – 2317

6

Turn

2323 – 2333

11

Helix

2334 – 2337

4

Turn

2342 – 2344

3

Helix

2350 – 2354

5

Turn

2355 – 2357

3

Helix

2361 – 2372

12

Turn

2373 – 2375

3

Beta strand

2376 – 2378

3

Turn

2380 – 2382

3

Beta strand

2384 – 2386

3

Helix

2388 – 2393

6

Helix

2399 – 2406

8

Beta strand

2414 – 2417

4

Turn

2418 – 2421

4

Beta strand

2422 – 2424

3

Helix

2426 – 2431

6

Turn

2437 – 2439

3

Beta strand

2442 – 2446

5

Beta strand

2619 – 2624

6

Turn

2625 – 2628

4

Beta strand

2629 – 2631

3

Helix

2633 – 2638

6

Helix

2644 – 2655

12

Turn

2656 – 2658

3

Beta strand

2659 – 2661

3

Turn

2663 – 2665

3

Helix

2671 – 2676

6

Helix

2682 – 2696

15

Helix

2709 – 2714

6

Helix

2720 – 2732

13

Helix

2739 – 2741

3

Helix

2747 – 2752

6

Helix

2758 – 2765

8

Helix

2767 – 2769

3

Turn

2777 – 2779

3

Helix

2785 – 2791

7

Turn

2796 – 2798

3

Beta strand

2801 – 2805

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform DPI (DP1) [UniParc]. Last modified October 3, 2006. Version 3. Checksum: 5770CC6B4F9F9F7B	FASTA	2,871	331,774
	10 20 30 40 50 60 MSCNGGSHPR INTLGRMIRA ESGPDLRYEV TSGGGGTSRM YYSRRGVITD QNSDGYCQTG 70 80 90 100 110 120 TMSRHQNQNT IQELLQNCSD CLMRAELIVQ PELKYGDGIQ LTRSRELDEC FAQANDQMEI 130 140 150 160 170 180 LDSLIREMRQ MGQPCDAYQK RLLQLQEQMR ALYKAISVPR VRRASSKGGG GYTCQSGSGW 190 200 210 220 230 240 DEFTKHVTSE CLGWMRQQRA EMDMVAWGVD LASVEQHINS HRGIHNSIGD YRWQLDKIKA 250 260 270 280 290 300 DLREKSAIYQ LEEEYENLLK ASFERMDHLR QLQNIIQATS REIMWINDCE EEELLYDWSD 310 320 330 340 350 360 KNTNIAQKQE AFSIRMSQLE VKEKELNKLK QESDQLVLNQ HPASDKIEAY MDTLQTQWSW 370 380 390 400 410 420 ILQITKCIDV HLKENAAYFQ FFEEAQSTEA YLKGLQDSIR KKYPCDKNMP LQHLLEQIKE 430 440 450 460 470 480 LEKEREKILE YKRQVQNLVN KSKKIVQLKP RNPDYRSNKP IILRALCDYK QDQKIVHKGD 490 500 510 520 530 540 ECILKDNNER SKWYVTGPGG VDMLVPSVGL IIPPPNPLAV DLSCKIEQYY EAILALWNQL 550 560 570 580 590 600 YINMKSLVSW HYCMIDIEKI RAMTIAKLKT MRQEDYMKTI ADLELHYQEF IRNSQGSEMF 610 620 630 640 650 660 GDDDKRKIQS QFTDAQKHYQ TLVIQLPGYP QHQTVTTTEI THHGTCQDVN HNKVIETNRE 670 680 690 700 710 720 NDKQETWMLM ELQKIRRQIE HCEGRMTLKN LPLADQGSSH HITVKINELK SVQNDSQAIA 730 740 750 760 770 780 EVLNQLKDML ANFRGSEKYC YLQNEVFGLF QKLENINGVT DGYLNSLCTV RALLQAILQT 790 800 810 820 830 840 EDMLKVYEAR LTEEETVCLD LDKVEAYRCG LKKIKNDLNL KKSLLATMKT ELQKAQQIHS 850 860 870 880 890 900 QTSQQYPLYD LDLGKFGEKV TQLTDRWQRI DKQIDFRLWD LEKQIKQLRN YRDNYQAFCK 910 920 930 940 950 960 WLYDAKRRQD SLESMKFGDS NTVMRFLNEQ KNLHSEISGK RDKSEEVQKI AELCANSIKD 970 980 990 1000 1010 1020 YELQLASYTS GLETLLNIPI KRTMIQSPSG VILQEAADVH ARYIELLTRS GDYYRFLSEM 1030 1040 1050 1060 1070 1080 LKSLEDLKLK NTKIEVLEEE LRLARDANSE NCNKNKFLDQ NLQKYQAECS QFKAKLASLE 1090 1100 1110 1120 1130 1140 ELKRQAELDG KSAKQNLDKC YGQIKELNEK ITRLTYEIED EKRRRKSVED RFDQQKNDYD 1150 1160 1170 1180 1190 1200 QLQKARQCEK ENLGWQKLES EKAIKEKEYE IERLRVLLQE EGTRKREYEN ELAKVRNHYN 1210 1220 1230 1240 1250 1260 EEMSNLRNKY ETEINITKTT IKEISMQKED DSKNLRNQLD RLSRENRDLK DEIVRLNDSI 1270 1280 1290 1300 1310 1320 LQATEQRRRA EENALQQKAC GSEIMQKKQH LEIELKQVMQ QRSEDNARHK QSLEEAAKTI 1330 1340 1350 1360 1370 1380 QDKNKEIERL KAEFQEEAKR RWEYENELSK VRNNYDEEII SLKNQFETEI NITKTTIHQL 1390 1400 1410 1420 1430 1440 TMQKEEDTSG YRAQIDNLTR ENRSLSEEIK RLKNTLTQTT ENLRRVEEDI QQQKATGSEV 1450 1460 1470 1480 1490 1500 SQRKQQLEVE LRQVTQMRTE ESVRYKQSLD DAAKTIQDKN KEIERLKQLI DKETNDRKCL 1510 1520 1530 1540 1550 1560 EDENARLQRV QYDLQKANSS ATETINKLKV QEQELTRLRI DYERVSQERT VKDQDITRFQ 1570 1580 1590 1600 1610 1620 NSLKELQLQK QKVEEELNRL KRTASEDSCK RKKLEEELEG MRRSLKEQAI KITNLTQQLE 1630 1640 1650 1660 1670 1680 QASIVKKRSE DDLRQQRDVL DGHLREKQRT QEELRRLSSE VEALRRQLLQ EQESVKQAHL 1690 1700 1710 1720 1730 1740 RNEHFQKAIE DKSRSLNESK IEIERLQSLT ENLTKEHLML EEELRNLRLE YDDLRRGRSE 1750 1760 1770 1780 1790 1800 ADSDKNATIL ELRSQLQISN NRTLELQGLI NDLQRERENL RQEIEKFQKQ ALEASNRIQE 1810 1820 1830 1840 1850 1860 SKNQCTQVVQ ERESLLVKIK VLEQDKARLQ RLEDELNRAK STLEAETRVK QRLECEKQQI 1870 1880 1890 1900 1910 1920 QNDLNQWKTQ YSRKEEAIRK IESEREKSER EKNSLRSEIE RLQAEIKRIE ERCRRKLEDS 1930 1940 1950 1960 1970 1980 TRETQSQLET ERSRYQREID KLRQRPYGSH RETQTECEWT VDTSKLVFDG LRKKVTAMQL 1990 2000 2010 2020 2030 2040 YECQLIDKTT LDKLLKGKKS VEEVASEIQP FLRGAGSIAG ASASPKEKYS LVEAKRKKLI 2050 2060 2070 2080 2090 2100 SPESTVMLLE AQAATGGIID PHRNEKLTVD SAIARDLIDF DDRQQIYAAE KAITGFDDPF 2110 2120 2130 2140 2150 2160 SGKTVSVSEA IKKNLIDRET GMRLLEAQIA SGGVVDPVNS VFLPKDVALA RGLIDRDLYR 2170 2180 2190 2200 2210 2220 SLNDPRDSQK NFVDPVTKKK VSYVQLKERC RIEPHTGLLL LSVQKRSMSF QGIRQPVTVT 2230 2240 2250 2260 2270 2280 ELVDSGILRP STVNELESGQ ISYDEVGERI KDFLQGSSCI AGIYNETTKQ KLGIYEAMKI 2290 2300 2310 2320 2330 2340 GLVRPGTALE LLEAQAATGF IVDPVSNLRL PVEEAYKRGL VGIEFKEKLL SAERAVTGYN 2350 2360 2370 2380 2390 2400 DPETGNIISL FQAMNKELIE KGHGIRLLEA QIATGGIIDP KESHRLPVDI AYKRGYFNEE 2410 2420 2430 2440 2450 2460 LSEILSDPSD DTKGFFDPNT EENLTYLQLK ERCIKDEETG LCLLPLKEKK KQVQTSQKNT 2470 2480 2490 2500 2510 2520 LRKRRVVIVD PETNKEMSVQ EAYKKGLIDY ETFKELCEQE CEWEEITITG SDGSTRVVLV 2530 2540 2550 2560 2570 2580 DRKTGSQYDI QDAIDKGLVD RKFFDQYRSG SLSLTQFADM ISLKNGVGTS SSMGSGVSDD 2590 2600 2610 2620 2630 2640 VFSSSRHESV SKISTISSVR NLTIRSSSFS DTLEESSPIA AIFDTENLEK ISITEGIERG 2650 2660 2670 2680 2690 2700 IVDSITGQRL LEAQACTGGI IHPTTGQKLS LQDAVSQGVI DQDMATRLKP AQKAFIGFEG 2710 2720 2730 2740 2750 2760 VKGKKKMSAA EAVKEKWLPY EAGQRFLEFQ YLTGGLVDPE VHGRISTEEA IRKGFIDGRA 2770 2780 2790 2800 2810 2820 AQRLQDTSSY AKILTCPKTK LKISYKDAIN RSMVEDITGL RLLEAASVSS KGLPSPYNMS 2830 2840 2850 2860 2870 SAPGSRSGSR SGSRSGSRSG SRSGSRRGSF DATGNSSYSY SYSFSSSSIG H
	Isoform DPII (DP2) [UniParc]. Checksum: 84F0CD39B48E1339	FASTA	2,272	260,119
	10 20 30 40 50 60 MSCNGGSHPR INTLGRMIRA ESGPDLRYEV TSGGGGTSRM YYSRRGVITD QNSDGYCQTG 70 80 90 100 110 120 TMSRHQNQNT IQELLQNCSD CLMRAELIVQ PELKYGDGIQ LTRSRELDEC FAQANDQMEI 130 140 150 160 170 180 LDSLIREMRQ MGQPCDAYQK RLLQLQEQMR ALYKAISVPR VRRASSKGGG GYTCQSGSGW 190 200 210 220 230 240 DEFTKHVTSE CLGWMRQQRA EMDMVAWGVD LASVEQHINS HRGIHNSIGD YRWQLDKIKA 250 260 270 280 290 300 DLREKSAIYQ LEEEYENLLK ASFERMDHLR QLQNIIQATS REIMWINDCE EEELLYDWSD 310 320 330 340 350 360 KNTNIAQKQE AFSIRMSQLE VKEKELNKLK QESDQLVLNQ HPASDKIEAY MDTLQTQWSW 370 380 390 400 410 420 ILQITKCIDV HLKENAAYFQ FFEEAQSTEA YLKGLQDSIR KKYPCDKNMP LQHLLEQIKE 430 440 450 460 470 480 LEKEREKILE YKRQVQNLVN KSKKIVQLKP RNPDYRSNKP IILRALCDYK QDQKIVHKGD 490 500 510 520 530 540 ECILKDNNER SKWYVTGPGG VDMLVPSVGL IIPPPNPLAV DLSCKIEQYY EAILALWNQL 550 560 570 580 590 600 YINMKSLVSW HYCMIDIEKI RAMTIAKLKT MRQEDYMKTI ADLELHYQEF IRNSQGSEMF 610 620 630 640 650 660 GDDDKRKIQS QFTDAQKHYQ TLVIQLPGYP QHQTVTTTEI THHGTCQDVN HNKVIETNRE 670 680 690 700 710 720 NDKQETWMLM ELQKIRRQIE HCEGRMTLKN LPLADQGSSH HITVKINELK SVQNDSQAIA 730 740 750 760 770 780 EVLNQLKDML ANFRGSEKYC YLQNEVFGLF QKLENINGVT DGYLNSLCTV RALLQAILQT 790 800 810 820 830 840 EDMLKVYEAR LTEEETVCLD LDKVEAYRCG LKKIKNDLNL KKSLLATMKT ELQKAQQIHS 850 860 870 880 890 900 QTSQQYPLYD LDLGKFGEKV TQLTDRWQRI DKQIDFRLWD LEKQIKQLRN YRDNYQAFCK 910 920 930 940 950 960 WLYDAKRRQD SLESMKFGDS NTVMRFLNEQ KNLHSEISGK RDKSEEVQKI AELCANSIKD 970 980 990 1000 1010 1020 YELQLASYTS GLETLLNIPI KRTMIQSPSG VILQEAADVH ARYIELLTRS GDYYRFLSEM 1030 1040 1050 1060 1070 1080 LKSLEDLKLK NTKIEVLEEE LRLARDANSE NCNKNKFLDQ NLQKYQAECS QFKAKLASLE 1090 1100 1110 1120 1130 1140 ELKRQAELDG KSAKQNLDKC YGQIKELNEK ITRLTYEIED EKRRRKSVED RFDQQKNDYD 1150 1160 1170 1180 1190 1200 QLQKARQCEK ENLGWQKLES EKAIKEKEYE IERLRVLLQE EGTRKREYEN ELAKASNRIQ 1210 1220 1230 1240 1250 1260 ESKNQCTQVV QERESLLVKI KVLEQDKARL QRLEDELNRA KSTLEAETRV KQRLECEKQQ 1270 1280 1290 1300 1310 1320 IQNDLNQWKT QYSRKEEAIR KIESEREKSE REKNSLRSEI ERLQAEIKRI EERCRRKLED 1330 1340 1350 1360 1370 1380 STRETQSQLE TERSRYQREI DKLRQRPYGS HRETQTECEW TVDTSKLVFD GLRKKVTAMQ 1390 1400 1410 1420 1430 1440 LYECQLIDKT TLDKLLKGKK SVEEVASEIQ PFLRGAGSIA GASASPKEKY SLVEAKRKKL 1450 1460 1470 1480 1490 1500 ISPESTVMLL EAQAATGGII DPHRNEKLTV DSAIARDLID FDDRQQIYAA EKAITGFDDP 1510 1520 1530 1540 1550 1560 FSGKTVSVSE AIKKNLIDRE TGMRLLEAQI ASGGVVDPVN SVFLPKDVAL ARGLIDRDLY 1570 1580 1590 1600 1610 1620 RSLNDPRDSQ KNFVDPVTKK KVSYVQLKER CRIEPHTGLL LLSVQKRSMS FQGIRQPVTV 1630 1640 1650 1660 1670 1680 TELVDSGILR PSTVNELESG QISYDEVGER IKDFLQGSSC IAGIYNETTK QKLGIYEAMK 1690 1700 1710 1720 1730 1740 IGLVRPGTAL ELLEAQAATG FIVDPVSNLR LPVEEAYKRG LVGIEFKEKL LSAERAVTGY 1750 1760 1770 1780 1790 1800 NDPETGNIIS LFQAMNKELI EKGHGIRLLE AQIATGGIID PKESHRLPVD IAYKRGYFNE 1810 1820 1830 1840 1850 1860 ELSEILSDPS DDTKGFFDPN TEENLTYLQL KERCIKDEET GLCLLPLKEK KKQVQTSQKN 1870 1880 1890 1900 1910 1920 TLRKRRVVIV DPETNKEMSV QEAYKKGLID YETFKELCEQ ECEWEEITIT GSDGSTRVVL 1930 1940 1950 1960 1970 1980 VDRKTGSQYD IQDAIDKGLV DRKFFDQYRS GSLSLTQFAD MISLKNGVGT SSSMGSGVSD 1990 2000 2010 2020 2030 2040 DVFSSSRHES VSKISTISSV RNLTIRSSSF SDTLEESSPI AAIFDTENLE KISITEGIER 2050 2060 2070 2080 2090 2100 GIVDSITGQR LLEAQACTGG IIHPTTGQKL SLQDAVSQGV IDQDMATRLK PAQKAFIGFE 2110 2120 2130 2140 2150 2160 GVKGKKKMSA AEAVKEKWLP YEAGQRFLEF QYLTGGLVDP EVHGRISTEE AIRKGFIDGR 2170 2180 2190 2200 2210 2220 AAQRLQDTSS YAKILTCPKT KLKISYKDAI NRSMVEDITG LRLLEAASVS SKGLPSPYNM 2230 2240 2250 2260 2270 SSAPGSRSGS RSGSRSGSRS GSRSGSRRGS FDATGNSSYS YSYSFSSSSI GH

References

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[1]	"Molecular structure of the human desmoplakin I and II amino terminus." Virata M.L.A., Wagner R.M., Parry D.A.D., Green K.J. Proc. Natl. Acad. Sci. U.S.A. 89:544-548(1992) [PubMed: 1731325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DPI). Tissue: Foreskin.
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DPII).
[4]	"Structure of the human desmoplakins. Implications for function in the desmosomal plaque." Green K.J., Parry D.A.D., Steinert P.M., Virata M.L.A., Wagner R.M., Angst B.D., Nilles L.A. J. Biol. Chem. 265:2603-2612(1990) [PubMed: 1689290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1120-2871 (ISOFORM DPI). Tissue: Foreskin.
[5]	Erratum Green K.J., Parry D.A.D., Steinert P.M., Virata M.L.A., Wagner R.M., Angst B.D., Nilles L.A. J. Biol. Chem. 265:11406-11407(1990) [PubMed: 2391353] [Abstract]
[6]	"Striate palmoplantar keratoderma resulting from desmoplakin haploinsufficiency." Whittock N.V., Ashton G.H., Dopping-Hepenstal P.J., Gratian M.J., Keane F.M., Eady R.A.J., McGrath J.A. J. Invest. Dermatol. 113:940-946(1999) [PubMed: 10594734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2854-2871. Tissue: Skin.
[7]	"The amino-terminal domain of desmoplakin binds to plakoglobin and clusters desmosomal cadherin-plakoglobin complexes." Kowalczyk A.P., Bornslaeger E.A., Borgwardt J.E., Palka H.L., Dhaliwal A.S., Corcoran C.M., Denning M.F., Green K.J. J. Cell Biol. 139:773-784(1997) [PubMed: 9348293] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope." Marekov L.N., Steinert P.M. J. Biol. Chem. 273:17763-17770(1998) [PubMed: 9651377] [Abstract] Cited for: LIPIDATION.
[9]	"Haploinsufficiency of desmoplakin causes a striate subtype of palmoplantar keratoderma." Armstrong D.K., McKenna K.E., Purkis P.E., Green K.J., Eady R.A.J., Leigh I.M., Hughes A.E. Hum. Mol. Genet. 8:143-148(1999) [PubMed: 9887343] [Abstract] Cited for: INVOLVEMENT IN SPPK2.
[10]	Erratum Armstrong D.K., McKenna K.E., Purkis P.E., Green K.J., Eady R.A.J., Leigh I.M., Hughes A.E. Hum. Mol. Genet. 8:943-943(1999)
[11]	"Recessive mutation in desmoplakin disrupts desmoplakin-intermediate filament interactions and causes dilated cardiomyopathy, woolly hair and keratoderma." Norgett E.E., Hatsell S.J., Carvajal-Huerta L., Cabezas J.-C.R., Common J., Purkis P.E., Whittock N.V., Leigh I.M., Stevens H.P., Kelsell D.P. Hum. Mol. Genet. 9:2761-2766(2000) [PubMed: 11063735] [Abstract] Cited for: INVOLVEMENT IN DCWHK.
[12]	"Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly." Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A. J. Cell Sci. 116:387-399(2003) [PubMed: 12482924] [Abstract] Cited for: INTERACTION WITH COL17A1.
[13]	"Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus." Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H., Green K.J., Sonnenberg A., Borradori L. Mol. Biol. Cell 14:1978-1992(2003) [PubMed: 12802069] [Abstract] Cited for: ASSOCIATION WITH KERATIN FILAMENTS, MUTAGENESIS OF SER-2849, SUBCELLULAR LOCATION.
[14]	"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-176; SER-2024; SER-2209; SER-2815 AND SER-2825, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-22; SER-176; SER-2815; SER-2820 AND SER-2825, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[16]	"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. , 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-28; TYR-56 AND TYR-2275, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[17]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1220 AND SER-1225, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28 AND TYR-56, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[19]	"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-22 AND SER-2209, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2821, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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-2815 AND SER-2825, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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-2209, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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-22; SER-165; SER-166; SER-176; SER-2024; SER-2209; SER-2815; SER-2820; SER-2821; SER-2825; SER-2849; THR-2853; SER-2857 AND SER-2868, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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-178, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"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-56, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[26]	"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-2606, MASS SPECTROMETRY.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"Mechanistic insights into arrhythmogenic right ventricular cardiomyopathy caused by desmocollin-2 mutations." Gehmlich K., Syrris P., Peskett E., Evans A., Ehler E., Asimaki A., Anastasakis A., Tsatsopoulou A., Vouliotis A.I., Stefanadis C., Saffitz J.E., Protonotarios N., McKenna W.J. Cardiovasc. Res. 90:77-87(2011) [PubMed: 21062920] [Abstract] Cited for: INTERACTION WITH DSC2, VARIANT VAL-1833.
[29]	"Mutation in human desmoplakin domain binding to plakoglobin causes a dominant form of arrhythmogenic right ventricular cardiomyopathy." Rampazzo A., Nava A., Malacrida S., Beffagna G., Bauce B., Rossi V., Zimbello R., Simionati B., Basso C., Thiene G., Towbin J.A., Danieli G.A. Am. J. Hum. Genet. 71:1200-1206(2002) [PubMed: 12373648] [Abstract] Cited for: VARIANT ARVD8 ARG-299.
[30]	"Compound heterozygosity for non-sense and mis-sense mutations in desmoplakin underlies skin fragility/woolly hair syndrome." Whittock N.V., Wan H., Morley S.M., Garzon M.C., Kristal L., Hyde P., McLean W.H.I., Pulkkinen L., Uitto J., Christiano A.M., Eady R.A.J., McGrath J.A. J. Invest. Dermatol. 118:232-238(2002) [PubMed: 11841538] [Abstract] Cited for: VARIANTS SFWHS LYS-287 AND CYS-2366.
[31]	"A recessive mutation in desmoplakin causes arrhythmogenic right ventricular dysplasia, skin disorder, and woolly hair." Alcalai R., Metzger S., Rosenheck S., Meiner V., Chajek-Shaul T. J. Am. Coll. Cardiol. 42:319-327(2003) [PubMed: 12875771] [Abstract] Cited for: VARIANT ARRHYTHMOGENIC CARDIOMYOPATHY ARG-2375.
[32]	"Loss of desmoplakin tail causes lethal acantholytic epidermolysis bullosa." Jonkman M.F., Pasmooij A.M.G., Pasmans S.G.M.A., van den Berg M.P., Ter Horst H.J., Timmer A., Pas H.H. Am. J. Hum. Genet. 77:653-660(2005) [PubMed: 16175511] [Abstract] Cited for: INVOLVEMENT IN LETHAL ACANTHOLYTIC EPIDERMOLYSIS BULLOSA.
[33]	"Clinical profile of four families with arrhythmogenic right ventricular cardiomyopathy caused by dominant desmoplakin mutations." Bauce B., Basso C., Rampazzo A., Beffagna G., Daliento L., Frigo G., Malacrida S., Settimo L., Danieli G., Thiene G., Nava A. Eur. Heart J. 26:1666-1675(2005) [PubMed: 15941723] [Abstract] Cited for: VARIANTS ARVD8 ARG-299; LYS-1255 AND ILE-1775.
[34]	"Comprehensive desmosome mutation analysis in north americans with arrhythmogenic right ventricular dysplasia/cardiomyopathy." den Haan A.D., Tan B.Y., Zikusoka M.N., Llado L.I., Jain R., Daly A., Tichnell C., James C., Amat-Alarcon N., Abraham T., Russell S.D., Bluemke D.A., Calkins H., Dalal D., Judge D.P. Circ. Cardiovasc. Genet. 2:428-435(2009) [PubMed: 20031617] [Abstract] Cited for: VARIANTS ARVD8 ARG-299; LYS-1255 AND ILE-1775, VARIANTS PHE-305; VAL-1505; CYS-1512; LYS-1526; CYS-1537 AND GLN-1738.
[35]	"Role of genetic testing in arrhythmogenic right ventricular cardiomyopathy/dysplasia." Barahona-Dussault C., Benito B., Campuzano O., Iglesias A., Leung T.L., Robb L., Talajic M., Brugada R. Clin. Genet. 77:37-48(2010) [PubMed: 19863551] [Abstract] Cited for: VARIANTS PHE-305; CYS-1512; LYS-1526; CYS-1537; CYS-1537; GLN-1738 AND VAL-1833.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Desmoplakin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M77830 mRNA. Translation: AAA85135.1.
AL031058 Genomic DNA. Translation: CAA19927.1.
BC140802 mRNA. Translation: AAI40803.1.
J05211 mRNA. Translation: AAA35766.1.
AF139065 mRNA. Translation: AAF19785.1.

IPI

IPI00013933.
IPI00217182.

PIR

A38194.

RefSeq

NP_001008844.1. NM_001008844.1.
NP_004406.2. NM_004415.2.

UniGene

Hs.519873.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LM5	X-ray	1.80	A/B	2609-2822	[»]
1LM7	X-ray	3.00	A/B	2209-2456	[»]
3R6N	X-ray	2.95	A/B	178-627	[»]

ProteinModelPortal

P15924.

SMR

P15924. Positions 178-627, 2209-2448, 2613-2808.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-109N.

IntAct

P15924. 11 interactions.

MINT

MINT-1157663.

STRING

P15924.

PTM databases

PhosphoSite

P15924.

Polymorphism databases

DMDM

115502381.

Proteomic databases

PeptideAtlas

P15924.

PRIDE

P15924.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379802; ENSP00000369129; ENSG00000096696.

GeneID

1832.

KEGG

hsa:1832.

UCSC

uc003mxp.1. human.

Organism-specific databases

CTD

1832.

GeneCards

GC06P007541.

HGNC

HGNC:3052. DSP.

HPA

CAB037324.

MIM

125647. gene.
605676. phenotype.
607450. phenotype.
607655. phenotype.
609638. phenotype.
612908. phenotype.

neXtProt

NX_P15924.

Orphanet

217656. Familial isolated arrhythmogenic right ventricular dysplasia.
50942. Keratosis palmoplantaris striata.
158687. Lethal acantholytic epidermolysis bullosa.
65282. Woolly hair - palmoplantar keratoderma - dilated cardiomyopathy.

PharmGKB

PA27505.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17223.

GeneTree

ENSGT00550000074288.

HOGENOM

HBG445205.

HOVERGEN

HBG081434.

InParanoid

P15924.

OMA

KRSMSFQ.

OrthoDB

EOG43R3KR.

PhylomeDB

P15924.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P15924.

Bgee

P15924.

CleanEx

HS_DSP.

Genevestigator

P15924.

GermOnline

ENSG00000096696. Homo sapiens.

Family and domain databases

InterPro

IPR001101. Plectin_repeat.
IPR018159. Spectrin/alpha-actinin.
[Graphical view]

KO

K10381.

Pfam

PF00681. Plectin. 8 hits.
[Graphical view]

SMART

SM00250. PLEC. 18 hits.
SM00150. SPEC. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

7481.

SOURCE

Search...

Entry information

Entry name

DESP_HUMAN

Accession

Primary (citable) accession number: P15924
Secondary accession number(s): B2RTT2 , O75993, Q14189, Q9UHN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	October 3, 2006
Last modified:	January 25, 2012
This is version 153 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.