Q8TE73 (DYH5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynein heavy chain 5, axonemal

Alternative name(s):
Axonemal beta dynein heavy chain 5
Ciliary dynein heavy chain 5

Gene names

Name:	DNAH5
Synonyms:	DNAHC5, HL1, KIAA1603

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	4624 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required for structural and functional integrity of the cilia of ependymal cells lining the brain ventricles.
Subunit structure	Consists of at least two heavy chains and a number of intermediate and light chains.
Subcellular location	Cytoplasm › cytoskeleton › cilium axoneme.
Domain	Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.
Involvement in disease	Primary ciliary dyskinesia 3 (CILD3) [MIM:608644]: A disorder characterized by abnormalities of motile cilia. Respiratory infections leading to chronic inflammation and bronchiectasis are recurrent, due to defects in the respiratory cilia; reduced fertility is often observed in male patients due to abnormalities of sperm tails. Half of the patients exhibit randomization of left-right body asymmetry and situs inversus, due to dysfunction of monocilia at the embryonic node. Primary ciliary dyskinesia associated with situs inversus is referred to as Kartagener syndrome. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.6 Kartagener syndrome (KTGS) [MIM:244400]: An autosomal recessive disorder characterized by the association of primary ciliary dyskinesia with situs inversus. Clinical features include recurrent respiratory infections, bronchiectasis, infertility, and lateral transposition of the viscera of the thorax and abdomen. The situs inversus is most often total, although it can be partial in some cases (isolated dextrocardia or isolated transposition of abdominal viscera). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1
Sequence similarities	Belongs to the dynein heavy chain family.
Sequence caution	The sequence BAB15543.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell projection Cilium Cytoplasm Cytoskeleton Dynein Microtubule
Coding sequence diversity	Polymorphism
Disease	Ciliopathy Disease mutation Kartagener syndrome Primary ciliary dyskinesia
Domain	Coiled coil Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC ciliary or flagellar motility Inferred from electronic annotation. Source: Compara microtubule-based movement Inferred from electronic annotation. Source: InterPro
Cellular_component	axonemal dynein complex Inferred from electronic annotation. Source: Compara cilium axoneme Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: InterPro microtubule motor activity Non-traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 4624	4624	Dynein heavy chain 5, axonemal		PRO_0000114630
Regions
	Nucleotide binding	1980 – 1987	8	ATP Potential
	Nucleotide binding	2262 – 2269	8	ATP Potential
	Region	1 – 1941	1941	Stem By similarity
	Region	1942 – 2164	223	AAA 1 By similarity
	Region	2224 – 2443	220	AAA 2 By similarity
	Region	2550 – 2803	254	AAA 3 By similarity
	Region	2916 – 3170	255	AAA 4 By similarity
	Region	3185 – 3482	298	Stalk By similarity
	Region	3567 – 3797	231	AAA 5 By similarity
	Region	4012 – 4226	215	AAA 6 By similarity
	Coiled coil	284 – 305	22	Potential
	Coiled coil	740 – 825	86	Potential
	Coiled coil	1435 – 1465	31	Potential
	Coiled coil	3195 – 3302	108	Potential
	Coiled coil	3426 – 3491	66	Potential
	Coiled coil	3732 – 3817	86	Potential
	Coiled coil	4392 – 4420	29	Potential
Amino acid modifications
	Modified residue	163	1	Phosphoserine By similarity
Natural variations
	Natural variant	12	1	H → Q. Corresponds to variant rs339445 [ dbSNP | Ensembl ].		VAR_019603
	Natural variant	24	1	G → E. Corresponds to variant rs1530496 [ dbSNP | Ensembl ].		VAR_019604
	Natural variant	558	1	T → A. Corresponds to variant rs1530498 [ dbSNP | Ensembl ].		VAR_019605
	Natural variant	591	1	L → R. Corresponds to variant rs35090077 [ dbSNP | Ensembl ].		VAR_053840
	Natural variant	591	1	L → V. Corresponds to variant rs35090077 [ dbSNP | Ensembl ].		VAR_053841
	Natural variant	620	1	Q → K. Corresponds to variant rs34076967 [ dbSNP | Ensembl ].		VAR_053842
	Natural variant	765	1	K → N. Corresponds to variant rs4701997 [ dbSNP | Ensembl ].		VAR_053843
	Natural variant	766	1	I → L. Corresponds to variant rs4701997 [ dbSNP | Ensembl ].		VAR_027903
	Natural variant	1006	1	S → G. Corresponds to variant rs16902886 [ dbSNP | Ensembl ].		VAR_027904
	Natural variant	1081	1	M → V. Corresponds to variant rs16902880 [ dbSNP | Ensembl ].		VAR_027905
	Natural variant	1716	1	R → L in CILD3. Ref.6		VAR_030705
	Natural variant	2264	1	S → N in CILD3. Ref.6		VAR_030706
	Natural variant	2347	1	E → K in CILD3. Ref.6		VAR_030707
	Natural variant	2425	1	R → H. Corresponds to variant rs35900306 [ dbSNP | Ensembl ].		VAR_053844
	Natural variant	2463	1	Q → R. Corresponds to variant rs10078391 [ dbSNP | Ensembl ].		VAR_019606
	Natural variant	2501	1	R → P in CILD3. Ref.6		VAR_030708
	Natural variant	2843	1	F → S in CILD3. Ref.6		VAR_030709
	Natural variant	2862	1	L → F. Corresponds to variant rs10513155 [ dbSNP | Ensembl ].		VAR_019607
	Natural variant	3409	1	W → S in CILD3. Ref.6		VAR_030710
	Natural variant	3519	1	G → R in KTGS. Ref.1		VAR_019608
	Natural variant	3791	1	T → I. Corresponds to variant rs17263496 [ dbSNP | Ensembl ].		VAR_027906
	Natural variant	3843	1	S → L in CILD3. Ref.6		VAR_030711
	Natural variant	4134	1	A → V. Ref.4 Corresponds to variant rs30168 [ dbSNP | Ensembl ].		VAR_019609
	Natural variant	4205	1	G → V in CILD3. Ref.6		VAR_030712
	Natural variant	4220	1	T → A. Corresponds to variant rs2277046 [ dbSNP | Ensembl ].		VAR_019610
	Natural variant	4450	1	I → V. Ref.4 Ref.5 Corresponds to variant rs3734110 [ dbSNP | Ensembl ].		VAR_019611
Experimental info
	Sequence conflict	2000	1	Y → D in AAC50699. Ref.3
	Sequence conflict	2027	1	S → A in AAL06603. Ref.2
	Sequence conflict	2027	1	S → A in AAC50699. Ref.3
	Sequence conflict	2207	1	D → N in AAL06603. Ref.2
	Sequence conflict	2227	1	S → N in AAL06603. Ref.2
	Sequence conflict	2232	1	E → K in AAL06603. Ref.2
	Sequence conflict	2248 – 2250	3	LFE → QTK in AAL06603. Ref.2
	Sequence conflict	4429	1	R → Q in BAB15543. Ref.5
	Sequence conflict	4451	1	S → F in BAB15543. Ref.5
	Sequence conflict	4527	1	A → T in BAB15543. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8TE73 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: B9BC9F20A4C581BE	FASTA	4,624	529,021
	10 20 30 40 50 60 MFRIGRRQLW KHSVTRVLTQ RLKGEKEAKR ALLDARHNYL FAIVASCLDL NKTEVEDAIL 70 80 90 100 110 120 EGNQIERIDQ LFAVGGLRHL MFYYQDVEEA ETGQLGSLGG VNLVSGKIKK PKVFVTEGND 130 140 150 160 170 180 VALTGVCVFF IRTDPSKAIT PDNIHQEVSF NMLDAADGGL LNSVRRLLSD IFIPALRATS 190 200 210 220 230 240 HGWGELEGLQ DAANIRQEFL SSLEGFVNVL SGAQESLKEK VNLRKCDILE LKTLKEPTDY 250 260 270 280 290 300 LTLANNPETL GKIEDCMKVW IKQTEQVLAE NNQLLKEADD VGPRAELEHW KKRLSKFNYL 310 320 330 340 350 360 LEQLKSPDVK AVLAVLAAAK SKLLKTWREM DIRITDATNE AKDNVKYLYT LEKCCDPLYS 370 380 390 400 410 420 SDPLSMMDAI PTLINAIKMI YSISHYYNTS EKITSLFVKV TNQIISACKA YITNNGTASI 430 440 450 460 470 480 WNQPQDVVEE KILSAIKLKQ EYQLCFHKTK QKLKQNPNAK QFDFSEMYIF GKFETFHRRL 490 500 510 520 530 540 AKIIDIFTTL KTYSVLQDST IEGLEDMATK YQGIVATIKK KEYNFLDQRK MDFDQDYEEF 550 560 570 580 590 600 CKQTNDLHNE LRKFMDVTFA KIQNTNQALR MLKKFERLNI PNLGIDDKYQ LILENYGADI 610 620 630 640 650 660 DMISKLYTKQ KYDPPLARNQ PPIAGKILWA RQLFHRIQQP MQLFQQHPAV LSTAEAKPII 670 680 690 700 710 720 RSYNRMAKVL LEFEVLFHRA WLRQIEEIHV GLEASLLVKA PGTGELFVNF DPQILILFRE 730 740 750 760 770 780 TECMAQMGLE VSPLATSLFQ KRDRYKRNFS NMKMMLAEYQ RVKSKIPAAI EQLIVPHLAK 790 800 810 820 830 840 VDEALQPGLA ALTWTSLNIE AYLENTFAKI KDLELLLDRV NDLIEFRIDA ILEEMSSTPL 850 860 870 880 890 900 CQLPQEEPLT CEEFLQMTKD LCVNGAQILH FKSSLVEEAV NELVNMLLDV EVLSEEESEK 910 920 930 940 950 960 ISNENSVNYK NESSAKREEG NFDTLTSSIN ARANALLLTT VTRKKKETEM LGEEARELLS 970 980 990 1000 1010 1020 HFNHQNMDAL LKVTRNTLEA IRKRIHSSHT INFRDSNSAS NMKQNSLPIF RASVTLAIPN 1030 1040 1050 1060 1070 1080 IVMAPALEDV QQTLNKAVEC IISVPKGVRQ WSSELLSKKK IQERKMAALQ SNEDSDSDVE 1090 1100 1110 1120 1130 1140 MGENELQDTL EIASVNLPIP VQTKNYYKNV SENKEIVKLV SVLSTIINST KKEVITSMDC 1150 1160 1170 1180 1190 1200 FKRYNHIWQK GKEEAIKTFI TQSPLLSEFE SQILYFQNLE QEINAEPEYV CVGSIALYTA 1210 1220 1230 1240 1250 1260 DLKFALTAET KAWMVVIGRH CNKKYRSEME NIFMLIEEFN KKLNRPIKDL DDIRIAMAAL 1270 1280 1290 1300 1310 1320 KEIREEQISI DFQVGPIEES YALLNRYGLL IAREEIDKVD TLHYAWEKLL ARAGEVQNKL 1330 1340 1350 1360 1370 1380 VSLQPSFKKE LISAVEVFLQ DCHQFYLDYD LNGPMASGLK PQEASDRLIM FQNQFDNIYR 1390 1400 1410 1420 1430 1440 KYITYTGGEE LFGLPATQYP QLLEIKKQLN LLQKIYTLYN SVIETVNSYY DILWSEVNIE 1450 1460 1470 1480 1490 1500 KINNELLEFQ NRCRKLPRAL KDWQAFLDLK KIIDDFSECC PLLEYMASKA MMERHWERIT 1510 1520 1530 1540 1550 1560 TLTGHSLDVG NESFKLRNIM EAPLLKYKEE IEDICISAVK ERDIEQKLKQ VINEWDNKTF 1570 1580 1590 1600 1610 1620 TFGSFKTRGE LLLRGDSTSE IIANMEDSLM LLGSLLSNRY NMPFKAQIQK WVQYLSNSTD 1630 1640 1650 1660 1670 1680 IIESWMTVQN LWIYLEAVFV GGDIAKQLPK EAKRFSNIDK SWVKIMTRAH EVPSVVQCCV 1690 1700 1710 1720 1730 1740 GDETLGQLLP HLLDQLEICQ KSLTGYLEKK RLCFPRFFFV SDPALLEILG QASDSHTIQA 1750 1760 1770 1780 1790 1800 HLLNVFDNIK SVKFHEKIYD RILSISSQEG ETIELDKPVM AEGNVEVWLN SLLEESQSSL 1810 1820 1830 1840 1850 1860 HLVIRQAAAN IQETGFQLTE FLSSFPAQVG LLGIQMIWTR DSEEALRNAK FDKKIMQKTN 1870 1880 1890 1900 1910 1920 QAFLELLNTL IDVTTRDLSS TERVKYETLI TIHVHQRDIF DDLCHMHIKS PMDFEWLKQC 1930 1940 1950 1960 1970 1980 RFYFNEDSDK MMIHITDVAF IYQNEFLGCT DRLVITPLTD RCYITLAQAL GMSMGGAPAG 1990 2000 2010 2020 2030 2040 PAGTGKTETT KDMGRCLGKY VVVFNCSDQM DFRGLGRIFK GLAQSGSWGC FDEFNRIDLP 2050 2060 2070 2080 2090 2100 VLSVAAQQIS IILTCKKEHK KSFIFTDGDN VTMNPEFGLF LTMNPGYAGR QELPENLKIN 2110 2120 2130 2140 2150 2160 FRSVAMMVPD RQIIIRVKLA SCGFIDNVVL ARKFFTLYKL CEEQLSKQVH YDFGLRNILS 2170 2180 2190 2200 2210 2220 VLRTLGAAKR ANPMDTESTI VMRVLRDMNL SKLIDEDEPL FLSLIEDLFP NILLDKAGYP 2230 2240 2250 2260 2270 2280 ELEAAISRQV EEAGLINHPP WKLKVIQLFE TQRVRHGMMT LGPSGAGKTT CIHTLMRAMT 2290 2300 2310 2320 2330 2340 DCGKPHREMR MNPKAITAPQ MFGRLDVATN DWTDGIFSTL WRKTLRAKKG EHIWIILDGP 2350 2360 2370 2380 2390 2400 VDAIWIENLN SVLDDNKTLT LANGDRIPMA PNCKIIFEPH NIDNASPATV SRNGMVFMSS 2410 2420 2430 2440 2450 2460 SILDWSPILE GFLKKRSPQE AEILRQLYTE SFPDLYRFCI QNLEYKMEVL EAFVITQSIN 2470 2480 2490 2500 2510 2520 MLQGLIPLKE QGGEVSQAHL GRLFVFALLW SAGAALELDG RRRLELWLRS RPTGTLELPP 2530 2540 2550 2560 2570 2580 PAGPGDTAFD YYVAPDGTWT HWNTRTQEYL YPSDTTPEYG SILVPNVDNV RTDFLIQTIA 2590 2600 2610 2620 2630 2640 KQGKAVLLIG EQGTAKTVII KGFMSKYDPE CHMIKSLNFS SATTPLMFQR TIESYVDKRM 2650 2660 2670 2680 2690 2700 GTTYGPPAGK KMTVFIDDVN MPIINEWGDQ VTNEIVRQLM EQNGFYNLEK PGEFTSIVDI 2710 2720 2730 2740 2750 2760 QFLAAMIHPG GGRNDIPQRL KRQFSIFNCT LPSEASVDKI FGVIGVGHYC TQRGFSEEVR 2770 2780 2790 2800 2810 2820 DSVTKLVPLT RRLWQMTKIK MLPTPAKFHY VFNLRDLSRV WQGMLNTTSE VIKEPNDLLK 2830 2840 2850 2860 2870 2880 LWKHECKRVI ADRFTVSSDV TWFDKALVSL VEEEFGEEKK LLVDCGIDTY FVDFLRDAPE 2890 2900 2910 2920 2930 2940 AAGETSEEAD AETPKIYEPI ESFSHLKERL NMFLQLYNES IRGAGMDMVF FADAMVHLVK 2950 2960 2970 2980 2990 3000 ISRVIRTPQG NALLVGVGGS GKQSLTRLAS FIAGYVSFQI TLTRSYNTSN LMEDLKVLYR 3010 3020 3030 3040 3050 3060 TAGQQGKGIT FIFTDNEIKD ESFLEYMNNV LSSGEVSNLF ARDEIDEINS DLASVMKKEF 3070 3080 3090 3100 3110 3120 PRCLPTNENL HDYFMSRVRQ NLHIVLCFSP VGEKFRNRAL KFPALISGCT IDWFSRWPKD 3130 3140 3150 3160 3170 3180 ALVAVSEHFL TSYDIDCSLE IKKEVVQCMG SFQDGVAEKC VDYFQRFRRS THVTPKSYLS 3190 3200 3210 3220 3230 3240 FIQGYKFIYG EKHVEVRTLA NRMNTGLEKL KEASESVAAL SKELEAKEKE LQVANDKADM 3250 3260 3270 3280 3290 3300 VLKEVTMKAQ AAEKVKAEVQ KVKDRAQAIV DSISKDKAIA EEKLEAAKPA LEEAEAALQT 3310 3320 3330 3340 3350 3360 IRPSDIATVR TLGRPPHLIM RIMDCVLLLF QRKVSAVKID LEKSCTMPSW QESLKLMTAG 3370 3380 3390 3400 3410 3420 NFLQNLQQFP KDTINEEVIE FLSPYFEMPD YNIETAKRVC GNVAGLCSWT KAMASFFSIN 3430 3440 3450 3460 3470 3480 KEVLPLKANL VVQENRHLLA MQDLQKAQAE LDDKQAELDV VQAEYEQAMT EKQTLLEDAE 3490 3500 3510 3520 3530 3540 RCRHKMQTAS TLISGLAGEK ERWTEQSQEF AAQTKRLVGD VLLATAFLSY SGPFNQEFRD 3550 3560 3570 3580 3590 3600 LLLNDWRKEM KARKIPFGKN LNLSEMLIDA PTISEWNLQG LPNDDLSIQN GIIVTKASRY 3610 3620 3630 3640 3650 3660 PLLIDPQTQG KIWIKNKESR NELQITSLNH KYFRNHLEDS LSLGRPLLIE DVGEELDPAL 3670 3680 3690 3700 3710 3720 DNVLERNFIK TGSTFKVKVG DKEVDVLDGF RLYITTKLPN PAYTPEISAR TSIIDFTVTM 3730 3740 3750 3760 3770 3780 KGLEDQLLGR VILTEKQELE KERTHLMEDV TANKRRMKEL EDNLLYRLTS TQGSLVEDES 3790 3800 3810 3820 3830 3840 LIVVLSNTKR TAEEVTQKLE ISAETEVQIN SAREEYRPVA TRGSILYFLI TEMRLVNEMY 3850 3860 3870 3880 3890 3900 QTSLRQFLGL FDLSLARSVK SPITSKRIAN IIEHMTYEVY KYAARGLYEE HKFLFTLLLT 3910 3920 3930 3940 3950 3960 LKIDIQRNRV KHEEFLTLIK GGASLDLKAC PPKPSKWILD ITWLNLVELS KLRQFSDVLD 3970 3980 3990 4000 4010 4020 QISRNEKMWK IWFDKENPEE EPLPNAYDKS LDCFRRLLLI RSWCPDRTIA QARKYIVDSM 4030 4040 4050 4060 4070 4080 GEKYAEGVIL DLEKTWEESD PRTPLICLLS MGSDPTDSII ALGKRLKIET RYVSMGQGQE 4090 4100 4110 4120 4130 4140 VHARKLLQQT MANGGWALLQ NCHLGLDFMD ELMDIIIETE LVHDAFRLWM TTEAHKQFPI 4150 4160 4170 4180 4190 4200 TLLQMSIKFA NDPPQGLRAG LKRTYSGVSQ DLLDVSSGSQ WKPMLYAVAF LHSTVQERRK 4210 4220 4230 4240 4250 4260 FGALGWNIPY EFNQADFNAT VQFIQNHLDD MDVKKGVSWT TIRYMIGEIQ YGGRVTDDYD 4270 4280 4290 4300 4310 4320 KRLLNTFAKV WFSENMFGPD FSFYQGYNIP KCSTVDNYLQ YIQSLPAYDS PEVFGLHPNA 4330 4340 4350 4360 4370 4380 DITYQSKLAK DVLDTILGIQ PKDTSGGGDE TREAVVARLA DDMLEKLPPD YVPFEVKERL 4390 4400 4410 4420 4430 4440 QKMGPFQPMN IFLRQEIDRM QRVLSLVRST LTELKLAIDG TIIMSENLRD ALDCMFDARI 4450 4460 4470 4480 4490 4500 PAWWKKASWI SSTLGFWFTE LIERNSQFTS WVFNGRPHCF WMTGFFNPQG FLTAMRQEIT 4510 4520 4530 4540 4550 4560 RANKGWALDN MVLCNEVTKW MKDDISAPPT EGVYVYGLYL EGAGWDKRNM KLIESKPKVL 4570 4580 4590 4600 4610 4620 FELMPVIRIY AENNTLRDPR FYSCPIYKKP VRTDLNYIAA VDLRTAQTPE HWVLRGVALL CDVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in DNAH5 cause primary ciliary dyskinesia and randomization of left-right asymmetry." Olbrich H., Haeffner K., Kispert A., Voelkel A., Volz A., Sasmaz G., Reinhardt R., Hennig S., Lehrach H., Konietzko N., Zariwala M., Noone P.G., Knowles M., Mitchison H.M., Meeks M., Chung E.M.K., Hildebrandt F., Sudbrak R., Omran H. Nat. Genet. 30:143-144(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT KTGS ARG-3519.
[2]	"Homozygosity mapping of a gene locus for primary ciliary dyskinesia on chromosome 5p and identification of the heavy dynein chain DNAH5 as a candidate gene." Omran H., Haeffner K., Voelkel A., Kuehr J., Ketelsen U.-P., Ross U.-H., Konietzko N., Wienker T., Brandis M., Hildebrandt F. Am. J. Respir. Cell Mol. Biol. 23:696-702(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1956-2469, INVOLVEMENT IN CILD3. Tissue: Testis.
[3]	"Multiple mouse chromosomal loci for dynein-based motility." Vaughan K.T., Mikami A., Paschal B.M., Holzbaur E.L.F., Hughes S.M., Echeverri C.J., Moore K.J., Gilbert D.J., Copeland N.G., Jenkins N.A., Vallee R.B. Genomics 36:29-38(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1956-2034. Tissue: Lung.
[4]	"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O. DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2966-4624, VARIANTS VAL-4134 AND VAL-4450. Tissue: Brain.
[5]	"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 4231-4602, VARIANT VAL-4450. Tissue: Lung.
[6]	"DNAH5 mutations are a common cause of primary ciliary dyskinesia with outer dynein arm defects." Hornef N., Olbrich H., Horvath J., Zariwala M.A., Fliegauf M., Loges N.T., Wildhaber J., Noone P.G., Kennedy M., Antonarakis S.E., Blouin J.-L., Bartoloni L., Nuesslein T., Ahrens P., Griese M., Kuhl H., Sudbrak R., Knowles M.R., Reinhardt R., Omran H. Am. J. Respir. Crit. Care Med. 174:120-126(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CILD3 LEU-1716; ASN-2264; LYS-2347; PRO-2501; SER-2843; SER-3409; LEU-3843 AND VAL-4205.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY045575 mRNA. Translation: AAK92217.1. AY049075 mRNA. Translation: AAL06603.1. U61735 mRNA. Translation: AAC50699.1. AB046823 mRNA. Translation: BAB13429.2. AK026756 mRNA. Translation: BAB15543.1. Different initiation.
IPI	IPI00152653.
RefSeq	NP_001360.1. NM_001369.2.
UniGene	Hs.212360.
3D structure databases
ProteinModelPortal	Q8TE73.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000265104.
PTM databases
PhosphoSite	Q8TE73.
Polymorphism databases
DMDM	116241343.
Proteomic databases
PaxDb	Q8TE73.
PeptideAtlas	Q8TE73.
PRIDE	Q8TE73.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265104; ENSP00000265104; ENSG00000039139.
GeneID	1767.
KEGG	hsa:1767.
UCSC	uc003jfd.2. human.
Organism-specific databases
CTD	1767.
GeneCards	GC05M013745.
HGNC	HGNC:2950. DNAH5.
HPA	HPA037469. HPA037470.
MIM	244400. phenotype. 603335. gene. 608644. phenotype.
neXtProt	NX_Q8TE73.
Orphanet	244. Primary ciliary dyskinesia.
PharmGKB	PA27403.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5245.
HOGENOM	HOG000257779.
HOVERGEN	HBG005543.
InParanoid	Q8TE73.
OMA	DLIEFRI.
OrthoDB	EOG4DNF3G.
PhylomeDB	Q8TE73.
Gene expression databases
ArrayExpress	Q8TE73.
Bgee	Q8TE73.
CleanEx	HS_DNAH5.
Genevestigator	Q8TE73.
GermOnline	ENSG00000039139. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR011704. ATPase_dyneun-rel_AAA. IPR026983. DHC_fam. IPR026978. DNAH5. IPR024743. Dynein_HC_stalk. IPR024317. Dynein_heavy_chain_D4_dom. IPR004273. Dynein_heavy_dom. IPR013594. Dynein_heavy_dom-1. IPR013602. Dynein_heavy_dom-2. [Graphical view]
PANTHER	PTHR10676. PTHR10676. 1 hit. PTHR10676:SF128. PTHR10676:SF128. 1 hit.
Pfam	PF07728. AAA_5. 1 hit. PF12780. AAA_8. 1 hit. PF08385. DHC_N1. 1 hit. PF08393. DHC_N2. 1 hit. PF03028. Dynein_heavy. 1 hit. PF12777. MT. 1 hit. [Graphical view]
SMART	SM00382. AAA. 3 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1767.
NextBio	7195.
SOURCE	Search...

Entry information

Entry name

DYH5_HUMAN

Accession

Primary (citable) accession number: Q8TE73
Secondary accession number(s): Q92860 , Q96L74, Q9H5S7, Q9HCG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 102 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.