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Protein

Cardiomyopathy-associated protein 5

Gene

CMYA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A (By similarity). May function as a repressor of calcineurin-mediated transcriptional activity. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration (By similarity).By similarity

Names & Taxonomyi

Protein namesi
Recommended name:
Cardiomyopathy-associated protein 5
Alternative name(s):
Dystrobrevin-binding protein 2
Genethonin-3
Myospryn
SPRY domain-containing protein 2
Tripartite motif-containing protein 76
Gene namesi
Name:CMYA5
Synonyms:C5orf10, DTNBP2, SPRYD2, TRIM76
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:14305. CMYA5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37868.

Polymorphism and mutation databases

BioMutaiCMYA5.
DMDMi182627649.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 40694069Cardiomyopathy-associated protein 5PRO_0000328722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei631 – 6311PhosphoserineBy similarity
Modified residuei2404 – 24041PhosphoserineBy similarity
Modified residuei2813 – 28131PhosphoserineBy similarity
Modified residuei3228 – 32281PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by PKA.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N3K9.
MaxQBiQ8N3K9.
PaxDbiQ8N3K9.
PeptideAtlasiQ8N3K9.
PRIDEiQ8N3K9.

PTM databases

iPTMnetiQ8N3K9.
PhosphoSiteiQ8N3K9.

Expressioni

Tissue specificityi

Expressed in skeletal muscle; at a strong level and in heart.1 Publication

Inductioni

Down-regulated in muscle cell lines derived from patients with Duchenne muscular dystrophy (DMD).2 Publications

Gene expression databases

BgeeiQ8N3K9.
CleanExiHS_CMYA5.
GenevisibleiQ8N3K9. HS.

Organism-specific databases

HPAiHPA037387.

Interactioni

Subunit structurei

Interacts with PRKAR2A (By similarity). Interacts with ACTN2 and DTNBP1/dysbindin (By similarity). Interacts with DES. Interacts with DMD/dystrophin (By similarity). Interacts with the calcineurin catalytic subunit PPP3CA (By similarity). Interacts with TTN. Interacts with CAPN3; this interaction, which results in CMYA5 proteolysis, may protect CAPN3 from autolysis.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DYSFO759233EBI-2323272,EBI-2799016

Protein-protein interaction databases

BioGridi128427. 9 interactions.
IntActiQ8N3K9. 9 interactions.
STRINGi9606.ENSP00000394770.

Structurei

3D structure databases

ProteinModelPortaliQ8N3K9.
SMRiQ8N3K9. Positions 3717-3895, 3905-4063.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3704 – 3805102Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini3806 – 389893Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini3880 – 4065186B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3517 – 354428Amphipathic helix H1Add
BLAST
Regioni3545 – 3672128B-box coiled-coil; BBCAdd
BLAST
Regioni3631 – 364818Amphipathic helix H2Add
BLAST
Regioni3751 – 376717Amphipathic helix H3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2964 – 298825Sequence analysisAdd
BLAST
Coiled coili3544 – 3653110Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 5738Glu-richAdd
BLAST
Compositional biasi483 – 639157Glu-richAdd
BLAST
Compositional biasi1584 – 15874Poly-Leu
Compositional biasi1918 – 19214Poly-Ser

Domaini

Amphipathic helix regions act as an anchoring domain for PKA, and appear to be responsible of the interaction between myospryn and PRKAR2A.

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG410ITEV. Eukaryota.
ENOG410YB7U. LUCA.
GeneTreeiENSGT00840000129812.
InParanoidiQ8N3K9.
OMAiDYGKKEI.
OrthoDBiEOG7RRF6F.
PhylomeDBiQ8N3K9.
TreeFamiTF331281.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50853. FN3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N3K9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRDSNHAG ESFLGSDGDE EATRELETEE ESEGEEDETA AESEEEPDSR
60 70 80 90 100
LSDQDEEGKI KQEYIISDPS FSMVTVQRED SGITWETNSS RSSTPWASEE
110 120 130 140 150
SQTSGVCSRE GSTVNSPPGN VSFIVDEVKK VRKRTHKSKH GSPSLRRKGN
160 170 180 190 200
RKRNSFESQD VPTNKKGSPL TSASQVLTTE KEKSYTGIYD KARKKKTTSN
210 220 230 240 250
TPPITGAIYK EHKPLVLRPV YIGTVQYKIK MFNSVKEELI PLQFYGTLPK
260 270 280 290 300
GYVIKEIHYR KGKDASISLE PDLDNSGSNT VSKTRKLVAQ SIEDKVKEVF
310 320 330 340 350
PPWRGALSKG SESLTLMFSH EDQKKIYADS PLNATSALEH TVPSYSSSGR
360 370 380 390 400
AEQGIQLRHS QSVPQQPEDE AKPHEVEPPS VTPDTPATMF LRTTKEECEL
410 420 430 440 450
ASPGTAASEN DSSVSPSFAN EVKKEDVYSA HHSISLEAAS PGLAASTQDG
460 470 480 490 500
LDPDQEQPDL TSIERAEPVS AKLTPTHPSV KGEKEENMLE PSISLSEPLM
510 520 530 540 550
LEEPEKEEIE TSLPIAITPE PEDSNLVEEE IVELDYPESP LVSEKPFPPH
560 570 580 590 600
MSPEVEHKEE ELILPLLAAS SPEHVALSEE EREEIASVST GSAFVSEYSV
610 620 630 640 650
PQDLNHELQE QEGEPVPPSN VEAIAEHAVL SEEENEEFEA YSPAAAPTSE
660 670 680 690 700
SSLSPSTTEK TSENQSPLFS TVTPEYMVLS GDEASESGCY TPDSTSASEY
710 720 730 740 750
SVPSLATKES LKKTIDRKSP LILKGVSEYM IPSEEKEDTG SFTPAVAPAS
760 770 780 790 800
EPSLSPSTTE KTSECQSPLP STATSEHVVP SEGEDLGSER FTPDSKLISK
810 820 830 840 850
YAAPLNATQE SQKKIINEAS QFKPKGISEH TVLSVDGKEV IGPSSPDLVV
860 870 880 890 900
ASEHSFPPHT TEMTSECQAP PLSATPSEYV VLSDEEAVEL ERYTPSSTSA
910 920 930 940 950
SEFSVPPYAT PEAQEEEIVH RSLNLKGASS PMNLSEEDQE DIGPFSPDSA
960 970 980 990 1000
FVSEFSFPPY ATQEAEKREF ECDSPICLTS PSEHTILSDE DTEEAELFSP
1010 1020 1030 1040 1050
DSASQVSIPP FRISETEKNE LEPDSLLTAV SASGYSCFSE ADEEDIGSTA
1060 1070 1080 1090 1100
ATPVSEQFSS SQKQKAETFP LMSPLEDLSL PPSTDKSEKA EIKPEIPTTS
1110 1120 1130 1140 1150
TSVSEYLILA QKQKTQAYLE PESEDLIPSH LTSEVEKGER EASSSVAAIP
1160 1170 1180 1190 1200
AALPAQSSIV KEETKPASPH SVLPDSVPAI KKEQEPTAAL TLKAADEQMA
1210 1220 1230 1240 1250
LSKVRKEEIV PDSQEATAHV SQDQKMEPQP PNVPESEMKY SVLPDMVDEP
1260 1270 1280 1290 1300
KKGVKPKLVL NVTSELEQRK LSKNEPEVIK PYSPLKETSL SGPEALSAVK
1310 1320 1330 1340 1350
MEMKHDSKIT TTPIVLHSAS SGVEKQVEHG PPALAFSALS EEIKKEIEPS
1360 1370 1380 1390 1400
SSTTTASVTK LDSNLTRAVK EEIPTDSSLI TPVDRPVLTK VGKGELGSGL
1410 1420 1430 1440 1450
PPLVTSADEH SVLAEEDKVA IKGASPIETS SKHLAWSEAE KEIKFDSLPS
1460 1470 1480 1490 1500
VSSIAEHSVL SEVEAKEVKA GLPVIKTSSS QHSDKSEEAR VEDKQDLLFS
1510 1520 1530 1540 1550
TVCDSERLVS SQKKSLMSTS EVLEPEHELP LSLWGEIKKK ETELPSSQNV
1560 1570 1580 1590 1600
SPASKHIIPK GKDEETASSS PELENLASGL APTLLLLSDD KNKPAVEVSS
1610 1620 1630 1640 1650
TAQGDFPSEK QDVALAELSL EPEKKDKPHQ PLELPNAGSE FSSDLGRQSG
1660 1670 1680 1690 1700
SIGTKQAKSP ITETEDSVLE KGPAELRSRE GKEENRELCA SSTMPAISEL
1710 1720 1730 1740 1750
SSLLREESQN EEIKPFSPKI ISLESKEPPA SVAEGGNPEE FQPFTFSLKG
1760 1770 1780 1790 1800
LSEEVSHPAD FKKGGNQEIG PLPPTGNLKA QVMGDILDKL SEETGHPNSS
1810 1820 1830 1840 1850
QVLQSITEPS KIAPSDLLVE QKKTEKALHS DQTVKLPDVS TSSEDKQDLG
1860 1870 1880 1890 1900
IKQFSLMREN LPLEQSKSFM TTKPADVKET KMEEFFISPK DENWMLGKPE
1910 1920 1930 1940 1950
NVASQHEQRI AGSVQLDSSS SNELRPGQLK AAVSSKDHTC EVRKQVLPHS
1960 1970 1980 1990 2000
AEESHLSSQE AVSALDTSSG NTETLSSKSY SSEEVKLAEE PKSLVLAGNV
2010 2020 2030 2040 2050
ERNIAEGKEI HSLMESESLL LEKANTELSW PSKEDSQEKI KLPPERFFQK
2060 2070 2080 2090 2100
PVSGLSVEQV KSETISSSVK TAHFPAEGVE PALGNEKEAH RSTPPFPEEK
2110 2120 2130 2140 2150
PLEESKMVQS KVIDDADEGK KPSPEVKIPT QRKPISSIHA REPQSPESPE
2160 2170 2180 2190 2200
VTQNPPTQPK VAKPDLPEEK GKKGISSFKS WMSSLFFGSS TPDNKVAEQE
2210 2220 2230 2240 2250
DLETQPSPSV EKAVTVIDPE GTIPTNFNVA EKPADHSLSE VKLKTADEPR
2260 2270 2280 2290 2300
GTLVKSGDGQ NVKEKSMILS NVEDLQQPKF ISEVSREDYG KKEISGDSEE
2310 2320 2330 2340 2350
MNINSVVTSA DGENLEIQSY SLIGEKLVME EAKTIVPPHV TDSKRVQKPA
2360 2370 2380 2390 2400
IAPPSKWNIS IFKEEPRSDQ KQKSLLSFDV VDKVPQQPKS ASSNFASKNI
2410 2420 2430 2440 2450
TKESEKPESI ILPVEESKGS LIDFSEDRLK KEMQNPTSLK ISEEETKLRS
2460 2470 2480 2490 2500
VSPTEKKDNL ENRSYTLAEK KVLAEKQNSV APLELRDSNE IGKTQITLGS
2510 2520 2530 2540 2550
RSTELKESKA DAMPQHFYQN EDYNERPKII VGSEKEKGEE KENQVYVLSE
2560 2570 2580 2590 2600
GKKQQEHQPY SVNVAESMSR ESDISLGHSL GETQSFSLVK ATSVTEKSEA
2610 2620 2630 2640 2650
MLAEAHPEIR EAKAVGTQPH PLEESKVLVE KTKTFLPVAL SCRDEIENHS
2660 2670 2680 2690 2700
LSQEGNLVLE KSSRDMPDHS EEKEQFRESE LSKGGSVDIT KETVKQGFQE
2710 2720 2730 2740 2750
KAVGTQPRPL EESKVLVEKT KTFLPVVLSC HDEIENHSLS QEGNLVLEKS
2760 2770 2780 2790 2800
SRDMPDHSEE KEQFKESELW KGGSVDITKE SMKEGFPSKE SERTLARPFD
2810 2820 2830 2840 2850
ETKSSETPPY LLSPVKPQTL ASGASPEINA VKKKEMPRSE LTPERHTVHT
2860 2870 2880 2890 2900
IQTSKDDTSD VPKQSVLVSK HHLEAAEDTR VKEPLSSAKS NYAQFISNTS
2910 2920 2930 2940 2950
ASNADKMVSN KEMPKEPEDT YAKGEDFTVT SKPAGLSEDQ KTAFSIISEG
2960 2970 2980 2990 3000
CEILNIHAPA FISSIDQEES EQMQDKLEYL EEKASFKTIP LPDDSETVAC
3010 3020 3030 3040 3050
HKTLKSRLED EKVTPLKENK QKETHKTKEE ISTDSETDLS FIQPTIPSEE
3060 3070 3080 3090 3100
DYFEKYTLID YNISPDPEKQ KAPQKLNVEE KLSKEVTEET ISFPVSSVES
3110 3120 3130 3140 3150
ALEHEYDLVK LDESFYGPEK GHNILSHPET QSQNSADRNV SKDTKRDVDS
3160 3170 3180 3190 3200
KSPGMPLFEA EEGVLSRTQI FPTTIKVIDP EFLEEPPALA FLYKDLYEEA
3210 3220 3230 3240 3250
VGEKKKEEET ASEGDSVNSE ASFPSRNSDT DDGTGIYFEK YILKDDILHD
3260 3270 3280 3290 3300
TSLTQKDQGQ GLEEKRVGKD DSYQPIAAEG EIWGKFGTIC REKSLEEQKG
3310 3320 3330 3340 3350
VYGEGESVDH VETVGNVAMQ KKAPITEDVR VATQKISYAV PFEDTHHVLE
3360 3370 3380 3390 3400
RADEAGSHGN EVGNASPEVN LNVPVQVSFP EEEFASGATH VQETSLEEPK
3410 3420 3430 3440 3450
ILVPPEPSEE RLRNSPVQDE YEFTESLHNE VVPQDILSEE LSSESTPEDV
3460 3470 3480 3490 3500
LSQGKESFEH ISENEFASEA EQSTPAEQKE LGSERKEEDQ LSSEVVTEKA
3510 3520 3530 3540 3550
QKELKKSQID TYCYTCKCPI SATDKVFGTH KDHEVSTLDT AISAVKVQLA
3560 3570 3580 3590 3600
EFLENLQEKS LRIEAFVSEI ESFFNTIEEN CSKNEKRLEE QNEEMMKKVL
3610 3620 3630 3640 3650
AQYDEKAQSF EEVKKKKMEF LHEQMVHFLQ SMDTAKDTLE TIVREAEELD
3660 3670 3680 3690 3700
EAVFLTSFEE INERLLSAME STASLEKMPA AFSLFEHYDD SSARSDQMLK
3710 3720 3730 3740 3750
QVAVPQPPRL EPQEPNSATS TTIAVYWSMN KEDVIDSFQV YCMEEPQDDQ
3760 3770 3780 3790 3800
EVNELVEEYR LTVKESYCIF EDLEPDRCYQ VWVMAVNFTG CSLPSERAIF
3810 3820 3830 3840 3850
RTAPSTPVIR AEDCTVCWNT ATIRWRPTTP EATETYTLEY CRQHSPEGEG
3860 3870 3880 3890 3900
LRSFSGIKGL QLKVNLQPND NYFFYVRAIN AFGTSEQSEA ALISTRGTRF
3910 3920 3930 3940 3950
LLLRETAHPA LHISSSGTVI SFGERRRLTE IPSVLGEELP SCGQHYWETT
3960 3970 3980 3990 4000
VTDCPAYRLG ICSSSAVQAG ALGQGETSWY MHCSEPQRYT FFYSGIVSDV
4010 4020 4030 4040 4050
HVTERPARVG ILLDYNNQRL IFINAESEQL LFIIRHRFNE GVHPAFALEK
4060
PGKCTLHLGI EPPDSVRHK
Length:4,069
Mass (Da):449,211
Last modified:April 8, 2008 - v3
Checksum:iF5A25F1C53640EB8
GO

Sequence cautioni

The sequence AAD55265.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH20856.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH22422.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH62664.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH63134.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI11530.1 differs from that shown. Reason: Erroneous termination at position 3283. Translated as Trp.Curated
The sequence AAQ09018.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH10406.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791E → D in CAH10406 (PubMed:17974005).Curated
Sequence conflicti445 – 4451A → V in CAH10406 (PubMed:17974005).Curated
Sequence conflicti616 – 6161V → I in CAH10402 (PubMed:17974005).Curated
Sequence conflicti654 – 6541S → L in CAH10406 (PubMed:17974005).Curated
Sequence conflicti924 – 9241N → D in CAH10402 (PubMed:17974005).Curated
Sequence conflicti995 – 9951A → T in CAH10406 (PubMed:17974005).Curated
Sequence conflicti1283 – 12831S → P in CAH10406 (PubMed:17974005).Curated
Sequence conflicti1606 – 16061F → L in CAH10406 (PubMed:17974005).Curated
Sequence conflicti1681 – 16811G → E in CAH10406 (PubMed:17974005).Curated
Sequence conflicti1855 – 18551S → G in AAH63134 (PubMed:15489334).Curated
Sequence conflicti2038 – 20381E → K in AAH63134 (PubMed:15489334).Curated
Sequence conflicti2148 – 21481S → A in AAD55265 (PubMed:11297942).Curated
Sequence conflicti2538 – 25381G → D in AAD55265 (PubMed:11297942).Curated
Sequence conflicti2782 – 27843MKE → TKD in CAD38607 (PubMed:17974005).Curated
Sequence conflicti2788 – 27881S → P in CAD38928 (PubMed:17974005).Curated
Sequence conflicti2933 – 29331P → L in CAD38607 (PubMed:17974005).Curated
Sequence conflicti3073 – 311341PQKLN…VKLDE → SFKTIPLPDDSETVACHKTL KSRLEDEKVTPLKENKQKET Q in AAH62664 (PubMed:15489334).CuratedAdd
BLAST
Sequence conflicti3131 – 31311Q → L in AAQ09018 (Ref. 6) Curated
Sequence conflicti3291 – 32911R → W in CAD91143 (PubMed:17974005).Curated
Sequence conflicti3321 – 33211K → R in CAD91143 (PubMed:17974005).Curated
Sequence conflicti3331 – 33311V → A in CAD91158 (PubMed:17974005).Curated
Sequence conflicti3348 – 33481V → A in CAD91158 (PubMed:17974005).Curated
Sequence conflicti3361 – 33611E → G in CAD91158 (PubMed:17974005).Curated
Sequence conflicti3803 – 382220APSTP…WNTAT → GKEMDAKGALEDNAQFFTDS in CAD91143 (PubMed:17974005).CuratedAdd
BLAST
Sequence conflicti3852 – 38521R → S in CAD91158 (PubMed:17974005).Curated
Sequence conflicti3880 – 38801N → S in CAD91158 (PubMed:17974005).Curated
Sequence conflicti3929 – 39291T → A in CAD91158 (PubMed:17974005).Curated
Sequence conflicti3948 – 39481E → K in CAD91158 (PubMed:17974005).Curated
Sequence conflicti4050 – 40501K → E in CAD38607 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641Y → C.
Corresponds to variant rs16877109 [ dbSNP | Ensembl ].
VAR_042471
Natural varianti175 – 1751Q → H.
Corresponds to variant rs6895605 [ dbSNP | Ensembl ].
VAR_042472
Natural varianti190 – 1901D → G.1 Publication
Corresponds to variant rs10942901 [ dbSNP | Ensembl ].
VAR_042473
Natural varianti349 – 3491G → D.
Corresponds to variant rs1366271 [ dbSNP | Ensembl ].
VAR_042474
Natural varianti591 – 5911G → D.
Corresponds to variant rs16877124 [ dbSNP | Ensembl ].
VAR_042475
Natural varianti651 – 6511S → R.
Corresponds to variant rs57544556 [ dbSNP | Ensembl ].
VAR_061611
Natural varianti1006 – 10061V → A.
Corresponds to variant rs6893869 [ dbSNP | Ensembl ].
VAR_042476
Natural varianti1295 – 12951A → V.1 Publication
Corresponds to variant rs4704585 [ dbSNP | Ensembl ].
VAR_042477
Natural varianti1309 – 13091I → V.
Corresponds to variant rs16877133 [ dbSNP | Ensembl ].
VAR_042478
Natural varianti1333 – 13331A → V.
Corresponds to variant rs16877135 [ dbSNP | Ensembl ].
VAR_042479
Natural varianti1380 – 13801I → V.
Corresponds to variant rs13158477 [ dbSNP | Ensembl ].
VAR_042480
Natural varianti1567 – 15671A → E.
Corresponds to variant rs1428223 [ dbSNP | Ensembl ].
VAR_042481
Natural varianti1599 – 15991S → A.
Corresponds to variant rs1428224 [ dbSNP | Ensembl ].
VAR_042482
Natural varianti1669 – 16691L → S.
Corresponds to variant rs1019762 [ dbSNP | Ensembl ].
VAR_042483
Natural varianti1713 – 17131I → N.
Corresponds to variant rs16877141 [ dbSNP | Ensembl ].
VAR_042484
Natural varianti1721 – 17211I → V.
Corresponds to variant rs1428225 [ dbSNP | Ensembl ].
VAR_042485
Natural varianti1875 – 18751A → V.
Corresponds to variant rs16877147 [ dbSNP | Ensembl ].
VAR_042486
Natural varianti1917 – 19171D → G.
Corresponds to variant rs16877150 [ dbSNP | Ensembl ].
VAR_042487
Natural varianti1920 – 19201S → G.1 Publication
Corresponds to variant rs16877151 [ dbSNP | Ensembl ].
VAR_042488
Natural varianti2262 – 22621V → L.1 Publication
Corresponds to variant rs6859595 [ dbSNP | Ensembl ].
VAR_042489
Natural varianti2383 – 23831K → E.
Corresponds to variant rs7721884 [ dbSNP | Ensembl ].
VAR_042490
Natural varianti2693 – 26931T → I.
Corresponds to variant rs28362541 [ dbSNP | Ensembl ].
VAR_042491
Natural varianti2906 – 29061K → N.
Corresponds to variant rs2278239 [ dbSNP | Ensembl ].
VAR_042492
Natural varianti2935 – 29351G → R.
Corresponds to variant rs2278240 [ dbSNP | Ensembl ].
VAR_042493
Natural varianti3358 – 33581H → Q.1 Publication
Corresponds to variant rs3828611 [ dbSNP | Ensembl ].
VAR_042494
Natural varianti3583 – 35831K → E.2 Publications
Corresponds to variant rs12514461 [ dbSNP | Ensembl ].
VAR_042495
Natural varianti3927 – 39271R → Q.2 Publications
Corresponds to variant rs1129770 [ dbSNP | Ensembl ].
VAR_042496
Natural varianti4063 – 40631P → L.1 Publication
Corresponds to variant rs10043986 [ dbSNP | Ensembl ].
VAR_042497

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008482 Genomic DNA. No translation available.
AC109488 Genomic DNA. No translation available.
AC008496 Genomic DNA. No translation available.
AL831966 mRNA. Translation: CAD38607.1.
AL831968 mRNA. Translation: CAD38609.2.
AL831986 mRNA. Translation: CAD91143.1.
AL832347 mRNA. Translation: CAH10406.1. Sequence problems.
AL832368 mRNA. Translation: CAD91158.1.
AL832376 mRNA. Translation: CAH10402.1.
AL834252 mRNA. Translation: CAD38928.2.
BC020856 mRNA. Translation: AAH20856.1. Sequence problems.
BC022422 mRNA. Translation: AAH22422.1. Sequence problems.
BC062664 mRNA. Translation: AAH62664.1. Sequence problems.
BC063134 mRNA. Translation: AAH63134.1. Sequence problems.
BC111529 mRNA. Translation: AAI11530.1. Sequence problems.
BC111530 mRNA. Translation: AAI11531.1.
AK092699 mRNA. No translation available.
AF177292 mRNA. Translation: AAD55265.1. Sequence problems.
AF533705 mRNA. Translation: AAQ09018.1. Different initiation.
CCDSiCCDS47238.1.
RefSeqiNP_705838.3. NM_153610.4.
UniGeneiHs.482625.

Genome annotation databases

EnsembliENST00000446378; ENSP00000394770; ENSG00000164309.
GeneIDi202333.
KEGGihsa:202333.
UCSCiuc003kgc.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008482 Genomic DNA. No translation available.
AC109488 Genomic DNA. No translation available.
AC008496 Genomic DNA. No translation available.
AL831966 mRNA. Translation: CAD38607.1.
AL831968 mRNA. Translation: CAD38609.2.
AL831986 mRNA. Translation: CAD91143.1.
AL832347 mRNA. Translation: CAH10406.1. Sequence problems.
AL832368 mRNA. Translation: CAD91158.1.
AL832376 mRNA. Translation: CAH10402.1.
AL834252 mRNA. Translation: CAD38928.2.
BC020856 mRNA. Translation: AAH20856.1. Sequence problems.
BC022422 mRNA. Translation: AAH22422.1. Sequence problems.
BC062664 mRNA. Translation: AAH62664.1. Sequence problems.
BC063134 mRNA. Translation: AAH63134.1. Sequence problems.
BC111529 mRNA. Translation: AAI11530.1. Sequence problems.
BC111530 mRNA. Translation: AAI11531.1.
AK092699 mRNA. No translation available.
AF177292 mRNA. Translation: AAD55265.1. Sequence problems.
AF533705 mRNA. Translation: AAQ09018.1. Different initiation.
CCDSiCCDS47238.1.
RefSeqiNP_705838.3. NM_153610.4.
UniGeneiHs.482625.

3D structure databases

ProteinModelPortaliQ8N3K9.
SMRiQ8N3K9. Positions 3717-3895, 3905-4063.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128427. 9 interactions.
IntActiQ8N3K9. 9 interactions.
STRINGi9606.ENSP00000394770.

PTM databases

iPTMnetiQ8N3K9.
PhosphoSiteiQ8N3K9.

Polymorphism and mutation databases

BioMutaiCMYA5.
DMDMi182627649.

Proteomic databases

EPDiQ8N3K9.
MaxQBiQ8N3K9.
PaxDbiQ8N3K9.
PeptideAtlasiQ8N3K9.
PRIDEiQ8N3K9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000446378; ENSP00000394770; ENSG00000164309.
GeneIDi202333.
KEGGihsa:202333.
UCSCiuc003kgc.4. human.

Organism-specific databases

CTDi202333.
GeneCardsiCMYA5.
H-InvDBHIX0004988.
HIX0004989.
HGNCiHGNC:14305. CMYA5.
HPAiHPA037387.
MIMi612193. gene.
neXtProtiNX_Q8N3K9.
PharmGKBiPA37868.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ITEV. Eukaryota.
ENOG410YB7U. LUCA.
GeneTreeiENSGT00840000129812.
InParanoidiQ8N3K9.
OMAiDYGKKEI.
OrthoDBiEOG7RRF6F.
PhylomeDBiQ8N3K9.
TreeFamiTF331281.

Miscellaneous databases

ChiTaRSiCMYA5. human.
GenomeRNAii202333.
PROiQ8N3K9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N3K9.
CleanExiHS_CMYA5.
GenevisibleiQ8N3K9. HS.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50853. FN3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1682 AND 2600-4069, VARIANTS GLY-190; VAL-1295; GLU-3583 AND LEU-4063.
    Tissue: Skeletal muscle.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-283; 1067-1340; 1604-2691 AND 2754-4069, VARIANTS GLY-1920; LEU-2262; GLN-3358; GLU-3583 AND GLN-3927.
    Tissue: Liver and Skeletal muscle.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1067-1340.
    Tissue: Skeletal muscle.
  5. "Identification of altered gene expression in skeletal muscles from Duchenne muscular dystrophy patients."
    Tkatchenko A.V., Pietu G., Cros N., Gannoun-Zaki L., Auffray C., Leger J.J., Dechesne C.A.
    Neuromuscul. Disord. 11:269-277(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1736-2539, INDUCTION, TISSUE SPECIFICITY.
  6. Ding P., Han W., Wang L., Wang Y., Qiu X., Xu M., Ma D.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3113-4069, VARIANT GLN-3927.
    Tissue: Mammary gland.
  7. "Myospryn is a novel binding partner for dysbindin in muscle."
    Benson M.A., Tinsley C.L., Blake D.J.
    J. Biol. Chem. 279:10450-10458(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Proper perinuclear localization of the TRIM-like protein myospryn requires its binding partner desmin."
    Kouloumenta A., Mavroidis M., Capetanaki Y.
    J. Biol. Chem. 282:35211-35221(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DES.
  9. "Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies."
    Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S., Milic A., Hackman P., Ehler E., Richard I., Udd B.
    J. Biol. Chem. 285:30304-30315(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CAPN3 AND TTN, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCMYA5_HUMAN
AccessioniPrimary (citable) accession number: Q8N3K9
Secondary accession number(s): A0PJB7
, Q05CT4, Q2NKX1, Q2T9G9, Q69YQ8, Q69YQ9, Q6P517, Q6P5U3, Q7Z4I1, Q86T34, Q86T49, Q8N3S4, Q8N3S7, Q8NAG8, Q9UK88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 8, 2008
Last modified: July 6, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.