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Protein

Cytoplasmic dynein 1 heavy chain 1

Gene

Dync1h1

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

Functioni

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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1904 – 1911ATPSequence analysis8
Nucleotide bindingi2222 – 2229ATPSequence analysis8
Nucleotide bindingi2593 – 2600ATPSequence analysis8
Nucleotide bindingi2935 – 2942ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

  • cilium movement Source: MGI
  • cytoplasmic mRNA processing body assembly Source: BHF-UCL
  • establishment of spindle localization Source: MGI
  • stress granule assembly Source: BHF-UCL
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2132295. MHC class II antigen presentation.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-MMU-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic dynein 1 heavy chain 1
Alternative name(s):
Cytoplasmic dynein heavy chain 1
Dynein heavy chain, cytosolic
Gene namesi
Name:Dync1h1
Synonyms:Dhc1, Dnch1, Dnchc1, Dyhc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:103147. Dync1h1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic dynein complex Source: MGI
  • extracellular exosome Source: MGI
  • extracellular matrix Source: MGI
  • filopodium Source: MGI
  • membrane Source: MGI
  • microtubule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

Pathology & Biotechi

Involvement in diseasei

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.

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.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001146282 – 4644Cytoplasmic dynein 1 heavy chain 1Add BLAST4643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei68PhosphoserineBy similarity1
Modified residuei1123N6-acetyllysineBy similarity1
Modified residuei1228PhosphoserineCombined sources1
Modified residuei3478N6-acetyllysineBy similarity1
Modified residuei4160PhosphoserineBy similarity1
Modified residuei4281N6-acetyllysineCombined sources1
Modified residuei4364PhosphothreonineBy similarity1
Modified residuei4366PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JHU4.
MaxQBiQ9JHU4.
PaxDbiQ9JHU4.
PeptideAtlasiQ9JHU4.
PRIDEiQ9JHU4.

PTM databases

iPTMnetiQ9JHU4.
PhosphoSitePlusiQ9JHU4.
SwissPalmiQ9JHU4.

Expressioni

Gene expression databases

BgeeiENSMUSG00000018707.
CleanExiMM_DYNC1H1.
ExpressionAtlasiQ9JHU4. baseline and differential.
GenevisibleiQ9JHU4. MM.

Interactioni

Subunit structurei

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). Interacts with BICD2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Csf1P071412EBI-645061,EBI-777188

GO - Molecular functioni

  • dynein light intermediate chain binding Source: MGI

Protein-protein interaction databases

BioGridi199254. 23 interactors.
IntActiQ9JHU4. 27 interactors.
MINTiMINT-1728570.
STRINGi10090.ENSMUSP00000018851.

Structurei

Secondary structure

14644
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3260 – 3295Combined sources36
Helixi3299 – 3306Combined sources8
Helixi3313 – 3325Combined sources13
Helixi3333 – 3336Combined sources4
Helixi3339 – 3341Combined sources3
Helixi3345 – 3351Combined sources7
Helixi3354 – 3356Combined sources3
Helixi3359 – 3368Combined sources10
Turni3369 – 3371Combined sources3
Helixi3377 – 3383Combined sources7
Helixi3387 – 3427Combined sources41
Turni3455 – 3457Combined sources3
Helixi3463 – 3467Combined sources5
Helixi3483 – 3485Combined sources3
Beta strandi3487 – 3493Combined sources7
Helixi3508 – 3514Combined sources7
Helixi3536 – 3541Combined sources6
Helixi3544 – 3557Combined sources14
Beta strandi3561 – 3564Combined sources4
Beta strandi3581 – 3583Combined sources3
Helixi3584 – 3590Combined sources7
Turni3597 – 3600Combined sources4
Helixi3601 – 3603Combined sources3
Beta strandi3605 – 3607Combined sources3
Beta strandi3610 – 3614Combined sources5
Helixi3795 – 3797Combined sources3
Beta strandi3799 – 3807Combined sources9
Beta strandi3826 – 3828Combined sources3
Helixi3830 – 3835Combined sources6
Beta strandi3838 – 3840Combined sources3
Beta strandi3848 – 3850Combined sources3
Beta strandi3852 – 3861Combined sources10
Helixi3863 – 3872Combined sources10
Helixi3883 – 3885Combined sources3
Helixi3886 – 3889Combined sources4
Beta strandi3893 – 3895Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ERRX-ray2.27A/B3260-3427[»]
3J1Telectron microscopy9.70A3264-3427[»]
3J1Uelectron microscopy9.70A3264-3427[»]
3WUQX-ray3.50A3207-3483[»]
5AYHX-ray3.01A3207-3475[»]
ProteinModelPortaliQ9JHU4.
SMRiQ9JHU4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHU4.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 1865StemBy similarityAdd BLAST1864
Regioni446 – 701Interaction with DYNC1I2By similarityAdd BLAST256
Regioni649 – 800Interaction with DYNC1LI2By similarityAdd BLAST152
Regioni1866 – 2097AAA 1By similarityAdd BLAST232
Regioni2178 – 2450AAA 2By similarityAdd BLAST273
Regioni2554 – 2803AAA 3By similarityAdd BLAST250
Regioni2897 – 3166AAA 4By similarityAdd BLAST270
Regioni3187 – 3498StalkBy similarityAdd BLAST312
Regioni3551 – 3780AAA 5By similarityAdd BLAST230
Regioni4003 – 4219AAA 6By similarityAdd BLAST217

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili48 – 69Sequence analysisAdd BLAST22
Coiled coili179 – 200Sequence analysisAdd BLAST22
Coiled coili453 – 476Sequence analysisAdd BLAST24
Coiled coili541 – 564Sequence analysisAdd BLAST24
Coiled coili1169 – 1201Sequence analysisAdd BLAST33
Coiled coili1229 – 1250Sequence analysisAdd BLAST22
Coiled coili1355 – 1371Sequence analysisAdd BLAST17
Coiled coili3187 – 3273Sequence analysisAdd BLAST87
Coiled coili3394 – 3498Sequence analysisAdd BLAST105
Coiled coili3735 – 3798Sequence analysisAdd BLAST64

Domaini

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.

Sequence similaritiesi

Belongs to the dynein heavy chain family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG3595. Eukaryota.
COG5245. LUCA.
GeneTreeiENSGT00760000118964.
HOGENOMiHOG000176055.
HOVERGENiHBG096595.
InParanoidiQ9JHU4.
KOiK10413.
OMAiMQIDQLE.
OrthoDBiEOG091G00JH.
TreeFamiTF101165.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011704. ATPase_dyneun-rel_AAA.
IPR026983. DHC_fam.
IPR024743. Dynein_HC_stalk.
IPR024317. Dynein_heavy_chain_D4_dom.
IPR004273. Dynein_heavy_dom.
IPR013594. Dynein_heavy_dom-1.
IPR013602. Dynein_heavy_dom-2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10676. PTHR10676. 3 hits.
PfamiPF07728. 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]
SMARTiSM00382. AAA. 4 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 5 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JHU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEPGGGEDG SAGLEVSAVQ NVADVAVLQK HLRKLVPLLL EDGGDAPAAL
60 70 80 90 100
EAALEEKSAL EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN
110 120 130 140 150
INIDIHYGVK SNSLAFIKRA PVIDADKPVS SQLRVLTLSE DSPYETLHSF
160 170 180 190 200
ISNAVAPFFK SYIRESGKAD RDGDKMAPSV EKKIAELEMG LLHLQQNIEI
210 220 230 240 250
PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL NQLQSGVNRW
260 270 280 290 300
IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD
310 320 330 340 350
ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK
360 370 380 390 400
IRQALVAIFT HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM
410 420 430 440 450
HVAYEEFEKV MVACFEVFQT WDDEYEKLQV LLRDIVKRKR EENLKMVWRI
460 470 480 490 500
NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR VLRPQVTAVA QQNQGEAPEP
510 520 530 540 550
QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG TEAWEAAMKR
560 570 580 590 600
YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR
610 620 630 640 650
EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK
660 670 680 690 700
QIDRQLTAYM KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW
710 720 730 740 750
ARKVQQRNLG VSGRIFTIES ARVRGRTGNV LKLKVNFLPE IITLSKEVRN
760 770 780 790 800
LKWLGFRVPL AIVNKAHQAN QLYPFAISLI ESVRTYERTC EKVEERNTIS
810 820 830 840 850
LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN FQEKVDDLLI
860 870 880 890 900
IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK
910 920 930 940 950
LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE
960 970 980 990 1000
PKIKNVVHEL RITNQVIYLN PPIEECRYKL YQEMFAWKMV VLSLPRIQSQ
1010 1020 1030 1040 1050
RYQVGVHYEL TEEEKFYRNA LTRMPDGPVA LEESYSAVMG IVTEVEQYVK
1060 1070 1080 1090 1100
VWLQYQCLWD MQAENIYNRL GEDLNKWQAL LVQIRKARGT FDNAETKKEF
1110 1120 1130 1140 1150
GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF HSQISKSRQE
1160 1170 1180 1190 1200
LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF
1210 1220 1230 1240 1250
QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES
1260 1270 1280 1290 1300
RTTDLLTDWE KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE
1310 1320 1330 1340 1350
ALELTDTGLL SGSEERVQVA LEELQDLKGV WSELSKVWEQ IDQMKEQPWV
1360 1370 1380 1390 1400
SVQPRKLRQN LDGLLNQLKN FPARLRQYAS YEFVQRLLKG YMKINMLVIE
1410 1420 1430 1440 1450
LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN EAVVKDVLLV
1460 1470 1480 1490 1500
AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN
1510 1520 1530 1540 1550
SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT
1560 1570 1580 1590 1600
GSADIKHLLP VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE
1610 1620 1630 1640 1650
RLADLLGKIQ KALGEYLERE RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK
1660 1670 1680 1690 1700
HFKKMFAGVS SIILNEDNSV VLGISSREGE EVMFKTPVSI TEHPKINEWL
1710 1720 1730 1740 1750
TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI DKYQAQLVVL
1760 1770 1780 1790 1800
SAQIAWSENV ENALSNVGGG GDVGPLQSVL SNVEVTLNVL ADSVLMEQPP
1810 1820 1830 1840 1850
LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD
1860 1870 1880 1890 1900
VLQQLSIQMA NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG
1910 1920 1930 1940 1950
SPFGPAGTGK TESVKALGHQ LGRFVLVFNC DETFDFQAMG RIFVGLCQVG
1960 1970 1980 1990 2000
AWGCFDEFNR LEERMLSAVS QQVQCIQEAL REHSNPNYDK TSAPITCELL
2010 2020 2030 2040 2050
NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT KPDRQLIAQV
2060 2070 2080 2090 2100
MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSAGN
2110 2120 2130 2140 2150
VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSVC ETMVPKLVAE
2160 2170 2180 2190 2200
DIPLLFSLLS DVFPGVQYHR GEMTALREEL KKVCQEMYLT YGDGEEVGGM
2210 2220 2230 2240 2250
WVEKVLQLYQ ITQINHGLMM VGPSGSGKSM AWRVLLKALE RLEGVEGVAH
2260 2270 2280 2290 2300
IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDNVR GELQKRQWIV
2310 2320 2330 2340 2350
FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM FEVQDLKYAT
2360 2370 2380 2390 2400
LATVSRCGMV WFSEDVLSTD MIFNNFLARL RSIPLDEGED EAQRRRKGKE
2410 2420 2430 2440 2450
DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL
2460 2470 2480 2490 2500
RCLGSLFSML HQACRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL
2510 2520 2530 2540 2550
SGDSRLKMRA ELGEYIRRIT TVPLPTAPNV PIIDYEVSIS GEWSPWQAKV
2560 2570 2580 2590 2600
PQIEVETHKV AAPDVVVPTL DTVRHEALLY TWLAEHKPLV LCGPPGSGKT
2610 2620 2630 2640 2650
MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR RTPNGVVLAP
2660 2670 2680 2690 2700
VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK
2710 2720 2730 2740 2750
LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN
2760 2770 2780 2790 2800
RAMLRLIPSL RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW
2810 2820 2830 2840 2850
VRGIFEALRP LETLPVEGLI RIWAHEALRL FQDRLVEDEE RRWTDENIDM
2860 2870 2880 2890 2900
VALKHFPNID KEKAMSRPIL YSNWLSKDYI PVDQEELRDY VKARLKVFYE
2910 2920 2930 2940 2950
EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG KTTLSRFVAW
2960 2970 2980 2990 3000
MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS
3010 3020 3030 3040 3050
GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK
3060 3070 3080 3090 3100
WFTSQVIRNL HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL
3110 3120 3130 3140 3150
YQVGKEFTSK MDLEKPNYIV PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ
3160 3170 3180 3190 3200
TLHQANARLA KRGGRTMAIT PRHYLDFINH YANLFHEKRS ELEEQQMHLN
3210 3220 3230 3240 3250
VGLRKIKETV DQVEELRRDL RIKSQELEVK NAAANDKLKK MVKDQQEAEK
3260 3270 3280 3290 3300
KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ
3310 3320 3330 3340 3350
HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV
3360 3370 3380 3390 3400
NFSAEEISDA IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY
3410 3420 3430 3440 3450
ADMLKRVEPL RNELQKLEDD AKDNQQKANE VEQMIRDLEA SIARYKEEYA
3460 3470 3480 3490 3500
VLISEAQAIK ADLAAVEAKV NRSTALLKSL SAERERWEKT SETFKNQMST
3510 3520 3530 3540 3550
IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ FRTDIARTEY
3560 3570 3580 3590 3600
LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN
3610 3620 3630 3640 3650
EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE
3660 3670 3680 3690 3700
VRRTGGRVLI TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT
3710 3720 3730 3740 3750
VTRSSLQSQC LNEVLKAERP DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA
3760 3770 3780 3790 3800
LNEVKGRILD DDTIITTLEN LKREAAEVTR KVEETDIVMQ EVETVSQQYL
3810 3820 3830 3840 3850
PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE NPNLKGATDH
3860 3870 3880 3890 3900
TQRLSIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD
3910 3920 3930 3940 3950
AEFQHFLRGK EIVLSAGSTP KIQGLTVEQA EAVVRLSCLP AFKDLIAKVQ
3960 3970 3980 3990 4000
ADEQFGIWLD SSSPEQTVPY LWSEETPTTP IGQAIHRLLL IQAFRPDRLL
4010 4020 4030 4040 4050
AMAHMFVSTN LGESFMSIME QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS
4060 4070 4080 4090 4100
GHVEDLAAEQ NTQITSIAIG SAEGFNQADK AINTAVKSGR WVMLKNVHLA
4110 4120 4130 4140 4150
PGWLMQLEKK LHSLQPHACF RLFLTMEINP KVPVNLLRAG RIFVFEPPPG
4160 4170 4180 4190 4200
VKANMLRTFS SIPVSRICKS PNERARLYFL LAWFHAIIQE RLRYAPLGWS
4210 4220 4230 4240 4250
KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY
4260 4270 4280 4290 4300
GGRVDNEFDQ RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR
4310 4320 4330 4340 4350
EEFVQWVELL PDAQTPSWLG LPNNAERVLL TTQGVDMISK MLKMQMLEDE
4360 4370 4380 4390 4400
DDLAYAETEK KARTDSTSDG RPAWMRTLHT TASNWLHLIP QTLSPLKRTV
4410 4420 4430 4440 4450
ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK KQTNYLRTLI
4460 4470 4480 4490 4500
NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAASGGAK
4510 4520 4530 4540 4550
ELKNIHVCLG GLFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSAT
4560 4570 4580 4590 4600
LDACSFGVTG LKLQGATCSN NKLSLSNAIS TVLPLTQLRW VKQTSAEKKA
4610 4620 4630 4640
SVVTLPVYLN FTRADLIFTV DFEIATKEDP RSFYERGVAV LCTE
Length:4,644
Mass (Da):532,045
Last modified:July 27, 2011 - v2
Checksum:iC88C9FC21D41DD56
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti517A → T in AAF91078 (Ref. 1) Curated1
Sequence conflicti2373F → L in AAF91078 (Ref. 1) Curated1
Sequence conflicti2689G → A in AAF91078 (Ref. 1) Curated1
Sequence conflicti3760D → V in AAF91078 (Ref. 1) Curated1
Sequence conflicti3856I → V in AAF91078 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti580F → Y in LOA. 1 Publication1
Natural varianti1055Y → C in CRA1. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY004877 mRNA. Translation: AAF91078.1.
AC152827 Genomic DNA. No translation available.
CCDSiCCDS36559.1.
RefSeqiNP_084514.2. NM_030238.2.
UniGeneiMm.181430.

Genome annotation databases

EnsembliENSMUST00000018851; ENSMUSP00000018851; ENSMUSG00000018707.
GeneIDi13424.
KEGGimmu:13424.
UCSCiuc007pbo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY004877 mRNA. Translation: AAF91078.1.
AC152827 Genomic DNA. No translation available.
CCDSiCCDS36559.1.
RefSeqiNP_084514.2. NM_030238.2.
UniGeneiMm.181430.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ERRX-ray2.27A/B3260-3427[»]
3J1Telectron microscopy9.70A3264-3427[»]
3J1Uelectron microscopy9.70A3264-3427[»]
3WUQX-ray3.50A3207-3483[»]
5AYHX-ray3.01A3207-3475[»]
ProteinModelPortaliQ9JHU4.
SMRiQ9JHU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199254. 23 interactors.
IntActiQ9JHU4. 27 interactors.
MINTiMINT-1728570.
STRINGi10090.ENSMUSP00000018851.

PTM databases

iPTMnetiQ9JHU4.
PhosphoSitePlusiQ9JHU4.
SwissPalmiQ9JHU4.

Proteomic databases

EPDiQ9JHU4.
MaxQBiQ9JHU4.
PaxDbiQ9JHU4.
PeptideAtlasiQ9JHU4.
PRIDEiQ9JHU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018851; ENSMUSP00000018851; ENSMUSG00000018707.
GeneIDi13424.
KEGGimmu:13424.
UCSCiuc007pbo.1. mouse.

Organism-specific databases

CTDi1778.
MGIiMGI:103147. Dync1h1.

Phylogenomic databases

eggNOGiKOG3595. Eukaryota.
COG5245. LUCA.
GeneTreeiENSGT00760000118964.
HOGENOMiHOG000176055.
HOVERGENiHBG096595.
InParanoidiQ9JHU4.
KOiK10413.
OMAiMQIDQLE.
OrthoDBiEOG091G00JH.
TreeFamiTF101165.

Enzyme and pathway databases

ReactomeiR-MMU-2132295. MHC class II antigen presentation.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-MMU-8854518. AURKA Activation by TPX2.

Miscellaneous databases

ChiTaRSiDync1h1. mouse.
EvolutionaryTraceiQ9JHU4.
PROiQ9JHU4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000018707.
CleanExiMM_DYNC1H1.
ExpressionAtlasiQ9JHU4. baseline and differential.
GenevisibleiQ9JHU4. MM.

Family and domain databases

Gene3Di3.40.50.300. 5 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011704. ATPase_dyneun-rel_AAA.
IPR026983. DHC_fam.
IPR024743. Dynein_HC_stalk.
IPR024317. Dynein_heavy_chain_D4_dom.
IPR004273. Dynein_heavy_dom.
IPR013594. Dynein_heavy_dom-1.
IPR013602. Dynein_heavy_dom-2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10676. PTHR10676. 3 hits.
PfamiPF07728. 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]
SMARTiSM00382. AAA. 4 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 5 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDYHC1_MOUSE
AccessioniPrimary (citable) accession number: Q9JHU4
Secondary accession number(s): E9QM71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.