Q9JHU4 (DYHC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoplasmic dynein 1 heavy chain 1

Alternative name(s):
Cytoplasmic dynein heavy chain 1
Dynein heavy chain, cytosolic

Gene names

Name:	Dync1h1
Synonyms:	Dhc1, Dnch1, Dnchc1, Dyhc

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	4644 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.
Subunit structure	Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and dynein LCs assemble on the IC dimer. Interacts with DYNC1LI1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with DYNC1LI2; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with DYNC1I2 By similarity.
Subcellular location	Cytoplasm.
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	Note=Defects in Dync1h1 are the cause of the 'Legs at odd angles' (LOA) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth. LOA mutants display defects in migration of facial motor neuron cell bodies and impaired retrograde transport in spinal cord motor neurons. Ref.4 Note=Defects in Dync1h1 are the cause of the Cramping 1 (Cra1) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth.
Sequence similarities	Belongs to the dynein heavy chain family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Dynein Microtubule
Disease	Disease mutation
Domain	Coiled coil Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	dynein complex Inferred from electronic annotation. Source: UniProtKB-KW 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 Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Csf1	P07141	1	EBI-645061,EBI-777188

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 4644

4644

Cytoplasmic dynein 1 heavy chain 1

PRO_0000114628

Regions

Nucleotide binding

1904 – 1911

8

ATP Potential

Nucleotide binding

2222 – 2229

8

ATP Potential

Nucleotide binding

2593 – 2600

8

ATP Potential

Nucleotide binding

2935 – 2942

8

ATP Potential

Region

1 – 1865

1865

Stem By similarity

Region

446 – 701

256

Interaction with DYNC1I2 By similarity

Region

649 – 800

152

Interaction with DYNC1LI2 By similarity

Region

1866 – 2097

232

AAA 1 By similarity

Region

2178 – 2450

273

AAA 2 By similarity

Region

2554 – 2803

250

AAA 3 By similarity

Region

2897 – 3166

270

AAA 4 By similarity

Region

3187 – 3498

312

Stalk By similarity

Region

3551 – 3780

230

AAA 5 By similarity

Region

4003 – 4219

217

AAA 6 By similarity

Coiled coil

48 – 69

22

Potential

Coiled coil

179 – 200

22

Potential

Coiled coil

453 – 476

24

Potential

Coiled coil

541 – 564

24

Potential

Coiled coil

1169 – 1201

33

Potential

Coiled coil

1229 – 1250

22

Potential

Coiled coil

1355 – 1371

17

Potential

Coiled coil

3187 – 3273

87

Potential

Coiled coil

3394 – 3498

105

Potential

Coiled coil

3735 – 3798

64

Potential

Amino acid modifications

Modified residue

369

1

N6-acetyllysine By similarity

Modified residue

392

1

N6-acetyllysine By similarity

Modified residue

752

1

N6-acetyllysine By similarity

Modified residue

1123

1

N6-acetyllysine By similarity

Modified residue

2408

1

Phosphoserine By similarity

Modified residue

2759

1

Phosphoserine By similarity

Modified residue

3377

1

Phosphotyrosine Ref.2

Modified residue

3478

1

N6-acetyllysine By similarity

Modified residue

4216

1

Phosphothreonine Ref.3

Modified residue

4219

1

Phosphothreonine Ref.3

Modified residue

4281

1

N6-acetyllysine By similarity

Modified residue

4366

1

Phosphoserine By similarity

Natural variations

Natural variant

580

1

F → Y in LOA. Ref.4

Natural variant

1055

1

Y → C in CRA1. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

4644

Helix Strand Turn

Details...

Helix

3260 – 3295

36

Helix

3299 – 3306

8

Helix

3313 – 3325

13

Helix

3333 – 3336

4

Helix

3339 – 3341

3

Helix

3345 – 3351

7

Helix

3354 – 3356

3

Helix

3359 – 3368

10

Turn

3369 – 3371

3

Helix

3377 – 3383

7

Helix

3390 – 3427

38

Sequences

	Sequence		Length	Mass (Da)
	Q9JHU4-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: FE5B4E15DD479E1B	FASTA	4,644	532,025
	10 20 30 40 50 60 MSEPGGGEDG SAGLEVSAVQ NVADVAVLQK HLRKLVPLLL EDGGDAPAAL EAALEEKSAL 70 80 90 100 110 120 EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN INIDIHYGVK SNSLAFIKRA 130 140 150 160 170 180 PVIDADKPVS SQLRVLTLSE DSPYETLHSF ISNAVAPFFK SYIRESGKAD RDGDKMAPSV 190 200 210 220 230 240 EKKIAELEMG LLHLQQNIEI PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL 250 260 270 280 290 300 NQLQSGVNRW IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD 310 320 330 340 350 360 ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK IRQALVAIFT 370 380 390 400 410 420 HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM HVAYEEFEKV MVACFEVFQT 430 440 450 460 470 480 WDDEYEKLQV LLRDIVKRKR EENLKMVWRI NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR 490 500 510 520 530 540 VLRPQVTAVA QQNQGEAPEP QDMKVAEVLF DAADANTIEE VNLAYENVKE VDGLDVSKEG 550 560 570 580 590 600 TEAWEAAMKR YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR 610 620 630 640 650 660 EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK QIDRQLTAYM 670 680 690 700 710 720 KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTIES 730 740 750 760 770 780 ARVRGRTGNV LKLKVNFLPE IITLSKEVRN LKWLGFRVPL AIVNKAHQAN QLYPFAISLI 790 800 810 820 830 840 ESVRTYERTC EKVEERNTIS LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN 850 860 870 880 890 900 FQEKVDDLLI IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK 910 920 930 940 950 960 LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE PKIKNVVHEL 970 980 990 1000 1010 1020 RITNQVIYLN PPIEECRYKL YQEMFAWKMV VLSLPRIQSQ RYQVGVHYEL TEEEKFYRNA 1030 1040 1050 1060 1070 1080 LTRMPDGPVA LEESYSAVMG IVTEVEQYVK VWLQYQCLWD MQAENIYNRL GEDLNKWQAL 1090 1100 1110 1120 1130 1140 LVQIRKARGT FDNAETKKEF GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF 1150 1160 1170 1180 1190 1200 HSQISKSRQE LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF 1210 1220 1230 1240 1250 1260 QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES RTTDLLTDWE 1270 1280 1290 1300 1310 1320 KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE ALELTDTGLL SGSEERVQVA 1330 1340 1350 1360 1370 1380 LEELQDLKGV WSELSKVWEQ IDQMKEQPWV SVQPRKLRQN LDGLLNQLKN FPARLRQYAS 1390 1400 1410 1420 1430 1440 YEFVQRLLKG YMKINMLVIE LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN 1450 1460 1470 1480 1490 1500 EAVVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN 1510 1520 1530 1540 1550 1560 SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT GSADIKHLLP 1570 1580 1590 1600 1610 1620 VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE RLADLLGKIQ KALGEYLERE 1630 1640 1650 1660 1670 1680 RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK HFKKMFAGVS SIILNEDNSV VLGISSREGE 1690 1700 1710 1720 1730 1740 EVMFKTPVSI TEHPKINEWL TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI 1750 1760 1770 1780 1790 1800 DKYQAQLVVL SAQIAWSENV ENALSNVGGG GDVGPLQSVL SNVEVTLNVL ADSVLMEQPP 1810 1820 1830 1840 1850 1860 LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD VLQQLSIQMA 1870 1880 1890 1900 1910 1920 NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG SPFGPAGTGK TESVKALGHQ 1930 1940 1950 1960 1970 1980 LGRFVLVFNC DETFDFQAMG RIFVGLCQVG AWGCFDEFNR LEERMLSAVS QQVQCIQEAL 1990 2000 2010 2020 2030 2040 REHSNPNYDK TSAPITCELL NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT 2050 2060 2070 2080 2090 2100 KPDRQLIAQV MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSAGN 2110 2120 2130 2140 2150 2160 VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSVC ETMVPKLVAE DIPLLFSLLS 2170 2180 2190 2200 2210 2220 DVFPGVQYHR GEMTALREEL KKVCQEMYLT YGDGEEVGGM WVEKVLQLYQ ITQINHGLMM 2230 2240 2250 2260 2270 2280 VGPSGSGKSM AWRVLLKALE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH 2290 2300 2310 2320 2330 2340 VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM 2350 2360 2370 2380 2390 2400 FEVQDLKYAT LATVSRCGMV WFSEDVLSTD MILNNFLARL RSIPLDEGED EAQRRRKGKE 2410 2420 2430 2440 2450 2460 DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL RCLGSLFSML 2470 2480 2490 2500 2510 2520 HQACRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL SGDSRLKMRA ELGEYIRRIT 2530 2540 2550 2560 2570 2580 TVPLPTAPNV PIIDYEVSIS GEWSPWQAKV PQIEVETHKV AAPDVVVPTL DTVRHEALLY 2590 2600 2610 2620 2630 2640 TWLAEHKPLV LCGPPGSGKT MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR 2650 2660 2670 2680 2690 2700 RTPNGVVLAP VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGAF YRTSDQTWVK 2710 2720 2730 2740 2750 2760 LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN RAMLRLIPSL 2770 2780 2790 2800 2810 2820 RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW VRGIFEALRP LETLPVEGLI 2830 2840 2850 2860 2870 2880 RIWAHEALRL FQDRLVEDEE RRWTDENIDM VALKHFPNID KEKAMSRPIL YSNWLSKDYI 2890 2900 2910 2920 2930 2940 PVDQEELRDY VKARLKVFYE EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG 2950 2960 2970 2980 2990 3000 KTTLSRFVAW MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS 3010 3020 3030 3040 3050 3060 GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK WFTSQVIRNL 3070 3080 3090 3100 3110 3120 HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNYIV 3130 3140 3150 3160 3170 3180 PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ TLHQANARLA KRGGRTMAIT PRHYLDFINH 3190 3200 3210 3220 3230 3240 YANLFHEKRS ELEEQQMHLN VGLRKIKETV DQVEELRRDL RIKSQELEVK NAAANDKLKK 3250 3260 3270 3280 3290 3300 MVKDQQEAEK KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ 3310 3320 3330 3340 3350 3360 HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV NFSAEEISDA 3370 3380 3390 3400 3410 3420 IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY ADMLKRVEPL RNELQKLEDD 3430 3440 3450 3460 3470 3480 AKDNQQKANE VEQMIRDLEA SIARYKEEYA VLISEAQAIK ADLAAVEAKV NRSTALLKSL 3490 3500 3510 3520 3530 3540 SAERERWEKT SETFKNQMST IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ 3550 3560 3570 3580 3590 3600 FRTDIARTEY LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN 3610 3620 3630 3640 3650 3660 EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE VRRTGGRVLI 3670 3680 3690 3700 3710 3720 TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT VTRSSLQSQC LNEVLKAERP 3730 3740 3750 3760 3770 3780 DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA LNEVKGRILV DDTIITTLEN LKREAAEVTR 3790 3800 3810 3820 3830 3840 KVEETDIVMQ EVETVSQQYL PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE 3850 3860 3870 3880 3890 3900 NPNLKGATDH TQRLSVITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD 3910 3920 3930 3940 3950 3960 AEFQHFLRGK EIVLSAGSTP KIQGLTVEQA EAVVRLSCLP AFKDLIAKVQ ADEQFGIWLD 3970 3980 3990 4000 4010 4020 SSSPEQTVPY LWSEETPTTP IGQAIHRLLL IQAFRPDRLL AMAHMFVSTN LGESFMSIME 4030 4040 4050 4060 4070 4080 QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS GHVEDLAAEQ NTQITSIAIG SAEGFNQADK 4090 4100 4110 4120 4130 4140 AINTAVKSGR WVMLKNVHLA PGWLMQLEKK LHSLQPHACF RLFLTMEINP KVPVNLLRAG 4150 4160 4170 4180 4190 4200 RIFVFEPPPG VKANMLRTFS SIPVSRICKS PNERARLYFL LAWFHAIIQE RLRYAPLGWS 4210 4220 4230 4240 4250 4260 KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY GGRVDNEFDQ 4270 4280 4290 4300 4310 4320 RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR EEFVQWVELL PDAQTPSWLG 4330 4340 4350 4360 4370 4380 LPNNAERVLL TTQGVDMISK MLKMQMLEDE DDLAYAETEK KARTDSTSDG RPAWMRTLHT 4390 4400 4410 4420 4430 4440 TASNWLHLIP QTLSPLKRTV ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK 4450 4460 4470 4480 4490 4500 KQTNYLRTLI NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAASGGAK 4510 4520 4530 4540 4550 4560 ELKNIHVCLG GLFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSAT LDACSFGVTG 4570 4580 4590 4600 4610 4620 LKLQGATCSN NKLSLSNAIS TVLPLTQLRW VKQTSAEKKA SVVTLPVYLN FTRADLIFTV 4630 4640 DFEIATKEDP RSFYERGVAV LCTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete cDNA sequence of murine cytoplasmic dynein heavy chain." Sasaki S., Shionoya A., Hirotsune S. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: FVB.
[2]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3377, MASS SPECTROMETRY. Tissue: Brain.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4216 AND THR-4219, MASS SPECTROMETRY. Tissue: Liver.
[4]	"Mutations in dynein link motor neuron degeneration to defects in retrograde transport." Hafezparast M., Klocke R., Ruhrberg C., Marquardt A., Ahmad-Annuar A., Bowen S., Lalli G., Witherden A.S., Hummerich H., Nicholson S., Morgan P.J., Oozageer R., Priestley J.V., Averill S., King V.R., Ball S., Peters J., Toda T. , Yamamoto A., Hiraoka Y., Augustin M., Korthaus D., Wattler S., Wabnitz P., Dickneite C., Lampel S., Boehme F., Peraus G., Popp A., Rudelius M., Schlegel J., Fuchs H., de Angelis M.H., Schiavo G., Shima D.T., Russ A.P., Stumm G., Martin J.E., Fisher E.M.C. Science 300:808-812(2003) [PubMed: 12730604] [Abstract] Cited for: VARIANT LOA TYR-580, VARIANT CRA1 CYS-1055.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY004877 mRNA. Translation: AAF91078.1.

IPI

IPI00119876.

UniGene

Mm.181430.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ERR	X-ray	2.27	A/B	3260-3427	[»]

ProteinModelPortal

Q9JHU4.

SMR

Q9JHU4. Positions 1903-1932, 2586-2747, 2931-2956.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9JHU4. 17 interactions.

STRING

Q9JHU4.

PTM databases

PhosphoSite

Q9JHU4.

Proteomic databases

PRIDE

Q9JHU4.

Genome annotation databases

Ensembl

ENSMUST00000018851; ENSMUSP00000018851; ENSMUSG00000018707; Mus musculus. [Genome view]

UCSC

uc007pbo.1. mouse.

Organism-specific databases

MGI

MGI:103147. Dync1h1.

Phylogenomic databases

HOGENOM

HBG358329.

HOVERGEN

HBG096595.

InParanoid

Q9JHU4.

PhylomeDB

Q9JHU4.

Gene expression databases

ArrayExpress

Q9JHU4.

Bgee

Q9JHU4.

CleanEx

MM_DYNC1H1.

Genevestigator

Q9JHU4.

GermOnline

ENSMUSG00000018707. Mus musculus.

Family and domain databases

InterPro

IPR003593. ATPase_AAA+_core.
IPR011704. ATPase_AAA-5.
IPR004273. Dynein_heavy.
IPR013594. Dynein_heavy_N-1.
IPR013602. Dynein_heavy_N-2.
[Graphical view]

Pfam

PF07728. AAA_5. 2 hits.
PF08385. DHC_N1. 1 hit.
PF08393. DHC_N2. 1 hit.
PF03028. Dynein_heavy. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

DYHC1_MOUSE

Accession

Primary (citable) accession number: Q9JHU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	October 1, 2000
Last modified:	August 10, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)