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Q9JHU4

- DYHC1_MOUSE

UniProt

Q9JHU4 - DYHC1_MOUSE

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Protein

Cytoplasmic dynein 1 heavy chain 1

Gene

Dync1h1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1904 – 19118ATPSequence Analysis
Nucleotide bindingi2222 – 22298ATPSequence Analysis
Nucleotide bindingi2593 – 26008ATPSequence Analysis
Nucleotide bindingi2935 – 29428ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. dynein light intermediate chain binding Source: MGI
  4. microtubule motor activity Source: InterPro
  5. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. cilium movement Source: MGI
  2. cytoplasmic mRNA processing body assembly Source: BHF-UCL
  3. stress granule assembly Source: BHF-UCL
  4. 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

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.

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
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:103147. Dync1h1.

Subcellular locationi

GO - Cellular componenti

  1. axonemal dynein complex Source: MGI
  2. centrosome Source: Ensembl
  3. cytoplasm Source: MGI
  4. extracellular vesicular exosome Source: Ensembl
  5. filopodium Source: MGI
  6. microtubule Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 46444643Cytoplasmic dynein 1 heavy chain 1PRO_0000114628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei1123 – 11231N6-acetyllysineBy similarity
Modified residuei3478 – 34781N6-acetyllysineBy similarity
Modified residuei4281 – 42811N6-acetyllysine1 Publication
Modified residuei4366 – 43661PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9JHU4.
PaxDbiQ9JHU4.
PRIDEiQ9JHU4.

PTM databases

PhosphoSiteiQ9JHU4.

Expressioni

Gene expression databases

BgeeiQ9JHU4.
CleanExiMM_DYNC1H1.
ExpressionAtlasiQ9JHU4. baseline and differential.
GenevestigatoriQ9JHU4.

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).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199254. 22 interactions.
IntActiQ9JHU4. 27 interactions.
MINTiMINT-1728570.

Structurei

Secondary structure

1
4644
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3260 – 329536Combined sources
Helixi3299 – 33068Combined sources
Helixi3313 – 332513Combined sources
Helixi3333 – 33364Combined sources
Helixi3339 – 33413Combined sources
Helixi3345 – 33517Combined sources
Helixi3354 – 33563Combined sources
Helixi3359 – 336810Combined sources
Turni3369 – 33713Combined sources
Helixi3377 – 33837Combined sources
Helixi3387 – 342741Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ERRX-ray2.27A/B3260-3427[»]
3J1Telectron microscopy9.70A3264-3427[»]
3J1Uelectron microscopy9.70A3264-3427[»]
3WUQX-ray3.50A3207-3483[»]
ProteinModelPortaliQ9JHU4.
SMRiQ9JHU4. Positions 3209-3471.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHU4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 18651864StemBy similarityAdd
BLAST
Regioni446 – 701256Interaction with DYNC1I2By similarityAdd
BLAST
Regioni649 – 800152Interaction with DYNC1LI2By similarityAdd
BLAST
Regioni1866 – 2097232AAA 1By similarityAdd
BLAST
Regioni2178 – 2450273AAA 2By similarityAdd
BLAST
Regioni2554 – 2803250AAA 3By similarityAdd
BLAST
Regioni2897 – 3166270AAA 4By similarityAdd
BLAST
Regioni3187 – 3498312StalkBy similarityAdd
BLAST
Regioni3551 – 3780230AAA 5By similarityAdd
BLAST
Regioni4003 – 4219217AAA 6By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili48 – 6922Sequence AnalysisAdd
BLAST
Coiled coili179 – 20022Sequence AnalysisAdd
BLAST
Coiled coili453 – 47624Sequence AnalysisAdd
BLAST
Coiled coili541 – 56424Sequence AnalysisAdd
BLAST
Coiled coili1169 – 120133Sequence AnalysisAdd
BLAST
Coiled coili1229 – 125022Sequence AnalysisAdd
BLAST
Coiled coili1355 – 137117Sequence AnalysisAdd
BLAST
Coiled coili3187 – 327387Sequence AnalysisAdd
BLAST
Coiled coili3394 – 3498105Sequence AnalysisAdd
BLAST
Coiled coili3735 – 379864Sequence AnalysisAdd
BLAST

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

eggNOGiCOG5245.
GeneTreeiENSGT00760000118964.
HOGENOMiHOG000176055.
HOVERGENiHBG096595.
InParanoidiQ9JHU4.
KOiK10413.
OMAiMQIDQLE.
OrthoDBiEOG76471R.
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. 1 hit.
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

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        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti517 – 5171A → T in AAF91078. 1 PublicationCurated
Sequence conflicti2373 – 23731F → L in AAF91078. 1 PublicationCurated
Sequence conflicti2689 – 26891G → A in AAF91078. 1 PublicationCurated
Sequence conflicti3760 – 37601D → V in AAF91078. 1 PublicationCurated
Sequence conflicti3856 – 38561I → V in AAF91078. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti580 – 5801F → Y in LOA. 1 Publication
Natural varianti1055 – 10551Y → C in CRA1. 1 Publication

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.
CCDSi CCDS36559.1.
RefSeqi NP_084514.2. NM_030238.2.
UniGenei Mm.181430.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ERR X-ray 2.27 A/B 3260-3427 [» ]
3J1T electron microscopy 9.70 A 3264-3427 [» ]
3J1U electron microscopy 9.70 A 3264-3427 [» ]
3WUQ X-ray 3.50 A 3207-3483 [» ]
ProteinModelPortali Q9JHU4.
SMRi Q9JHU4. Positions 3209-3471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199254. 22 interactions.
IntActi Q9JHU4. 27 interactions.
MINTi MINT-1728570.

PTM databases

PhosphoSitei Q9JHU4.

Proteomic databases

MaxQBi Q9JHU4.
PaxDbi Q9JHU4.
PRIDEi Q9JHU4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018851 ; ENSMUSP00000018851 ; ENSMUSG00000018707 .
GeneIDi 13424.
KEGGi mmu:13424.
UCSCi uc007pbo.1. mouse.

Organism-specific databases

CTDi 1778.
MGIi MGI:103147. Dync1h1.

Phylogenomic databases

eggNOGi COG5245.
GeneTreei ENSGT00760000118964.
HOGENOMi HOG000176055.
HOVERGENi HBG096595.
InParanoidi Q9JHU4.
KOi K10413.
OMAi MQIDQLE.
OrthoDBi EOG76471R.
TreeFami TF101165.

Enzyme and pathway databases

Reactomei REACT_196550. MHC class II antigen presentation.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.

Miscellaneous databases

ChiTaRSi Dync1h1. mouse.
EvolutionaryTracei Q9JHU4.
NextBioi 283839.
PROi Q9JHU4.
SOURCEi Search...

Gene expression databases

Bgeei Q9JHU4.
CleanExi MM_DYNC1H1.
ExpressionAtlasi Q9JHU4. baseline and differential.
Genevestigatori Q9JHU4.

Family and domain databases

Gene3Di 3.40.50.300. 5 hits.
InterProi IPR003593. 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 ]
PANTHERi PTHR10676. PTHR10676. 1 hit.
Pfami 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 ]
SMARTi SM00382. AAA. 4 hits.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 5 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  5. Cited for: VARIANT LOA TYR-580, VARIANT CRA1 CYS-1055.

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 26, 2014
This is version 126 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

External Data

Dasty 3