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Q9JHU4

- DYHC1_MOUSE

UniProt

Q9JHU4 - DYHC1_MOUSE

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
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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. protein binding Source: IntAct

    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

    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.

    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. Golgi apparatus Source: Ensembl
    7. microtubule Source: UniProtKB-KW

    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

    ArrayExpressiQ9JHU4.
    BgeeiQ9JHU4.
    CleanExiMM_DYNC1H1.
    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 – 329536
    Helixi3299 – 33068
    Helixi3313 – 332513
    Helixi3333 – 33364
    Helixi3339 – 33413
    Helixi3345 – 33517
    Helixi3354 – 33563
    Helixi3359 – 336810
    Turni3369 – 33713
    Helixi3377 – 33837
    Helixi3387 – 342741

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ERRX-ray2.27A/B3260-3427[»]
    3J1Telectron microscopy9.70A3264-3427[»]
    3J1Uelectron microscopy9.70A3264-3427[»]
    ProteinModelPortaliQ9JHU4.
    SMRiQ9JHU4. Positions 3264-3427.
    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.
    GeneTreeiENSGT00750000117443.
    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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    MSEPGGGEDG SAGLEVSAVQ NVADVAVLQK HLRKLVPLLL EDGGDAPAAL     50
    EAALEEKSAL EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN 100
    INIDIHYGVK SNSLAFIKRA PVIDADKPVS SQLRVLTLSE DSPYETLHSF 150
    ISNAVAPFFK SYIRESGKAD RDGDKMAPSV EKKIAELEMG LLHLQQNIEI 200
    PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL NQLQSGVNRW 250
    IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD 300
    ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK 350
    IRQALVAIFT HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM 400
    HVAYEEFEKV MVACFEVFQT WDDEYEKLQV LLRDIVKRKR EENLKMVWRI 450
    NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR VLRPQVTAVA QQNQGEAPEP 500
    QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG TEAWEAAMKR 550
    YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR 600
    EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK 650
    QIDRQLTAYM KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW 700
    ARKVQQRNLG VSGRIFTIES ARVRGRTGNV LKLKVNFLPE IITLSKEVRN 750
    LKWLGFRVPL AIVNKAHQAN QLYPFAISLI ESVRTYERTC EKVEERNTIS 800
    LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN FQEKVDDLLI 850
    IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK 900
    LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE 950
    PKIKNVVHEL RITNQVIYLN PPIEECRYKL YQEMFAWKMV VLSLPRIQSQ 1000
    RYQVGVHYEL TEEEKFYRNA LTRMPDGPVA LEESYSAVMG IVTEVEQYVK 1050
    VWLQYQCLWD MQAENIYNRL GEDLNKWQAL LVQIRKARGT FDNAETKKEF 1100
    GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF HSQISKSRQE 1150
    LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF 1200
    QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES 1250
    RTTDLLTDWE KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE 1300
    ALELTDTGLL SGSEERVQVA LEELQDLKGV WSELSKVWEQ IDQMKEQPWV 1350
    SVQPRKLRQN LDGLLNQLKN FPARLRQYAS YEFVQRLLKG YMKINMLVIE 1400
    LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN EAVVKDVLLV 1450
    AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN 1500
    SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT 1550
    GSADIKHLLP VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE 1600
    RLADLLGKIQ KALGEYLERE RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK 1650
    HFKKMFAGVS SIILNEDNSV VLGISSREGE EVMFKTPVSI TEHPKINEWL 1700
    TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI DKYQAQLVVL 1750
    SAQIAWSENV ENALSNVGGG GDVGPLQSVL SNVEVTLNVL ADSVLMEQPP 1800
    LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD 1850
    VLQQLSIQMA NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG 1900
    SPFGPAGTGK TESVKALGHQ LGRFVLVFNC DETFDFQAMG RIFVGLCQVG 1950
    AWGCFDEFNR LEERMLSAVS QQVQCIQEAL REHSNPNYDK TSAPITCELL 2000
    NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT KPDRQLIAQV 2050
    MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSAGN 2100
    VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSVC ETMVPKLVAE 2150
    DIPLLFSLLS DVFPGVQYHR GEMTALREEL KKVCQEMYLT YGDGEEVGGM 2200
    WVEKVLQLYQ ITQINHGLMM VGPSGSGKSM AWRVLLKALE RLEGVEGVAH 2250
    IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDNVR GELQKRQWIV 2300
    FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM FEVQDLKYAT 2350
    LATVSRCGMV WFSEDVLSTD MIFNNFLARL RSIPLDEGED EAQRRRKGKE 2400
    DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL 2450
    RCLGSLFSML HQACRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL 2500
    SGDSRLKMRA ELGEYIRRIT TVPLPTAPNV PIIDYEVSIS GEWSPWQAKV 2550
    PQIEVETHKV AAPDVVVPTL DTVRHEALLY TWLAEHKPLV LCGPPGSGKT 2600
    MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR RTPNGVVLAP 2650
    VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK 2700
    LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN 2750
    RAMLRLIPSL RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW 2800
    VRGIFEALRP LETLPVEGLI RIWAHEALRL FQDRLVEDEE RRWTDENIDM 2850
    VALKHFPNID KEKAMSRPIL YSNWLSKDYI PVDQEELRDY VKARLKVFYE 2900
    EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG KTTLSRFVAW 2950
    MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS 3000
    GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK 3050
    WFTSQVIRNL HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL 3100
    YQVGKEFTSK MDLEKPNYIV PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ 3150
    TLHQANARLA KRGGRTMAIT PRHYLDFINH YANLFHEKRS ELEEQQMHLN 3200
    VGLRKIKETV DQVEELRRDL RIKSQELEVK NAAANDKLKK MVKDQQEAEK 3250
    KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ 3300
    HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV 3350
    NFSAEEISDA IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY 3400
    ADMLKRVEPL RNELQKLEDD AKDNQQKANE VEQMIRDLEA SIARYKEEYA 3450
    VLISEAQAIK ADLAAVEAKV NRSTALLKSL SAERERWEKT SETFKNQMST 3500
    IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ FRTDIARTEY 3550
    LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN 3600
    EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE 3650
    VRRTGGRVLI TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT 3700
    VTRSSLQSQC LNEVLKAERP DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA 3750
    LNEVKGRILD DDTIITTLEN LKREAAEVTR KVEETDIVMQ EVETVSQQYL 3800
    PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE NPNLKGATDH 3850
    TQRLSIITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD 3900
    AEFQHFLRGK EIVLSAGSTP KIQGLTVEQA EAVVRLSCLP AFKDLIAKVQ 3950
    ADEQFGIWLD SSSPEQTVPY LWSEETPTTP IGQAIHRLLL IQAFRPDRLL 4000
    AMAHMFVSTN LGESFMSIME QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS 4050
    GHVEDLAAEQ NTQITSIAIG SAEGFNQADK AINTAVKSGR WVMLKNVHLA 4100
    PGWLMQLEKK LHSLQPHACF RLFLTMEINP KVPVNLLRAG RIFVFEPPPG 4150
    VKANMLRTFS SIPVSRICKS PNERARLYFL LAWFHAIIQE RLRYAPLGWS 4200
    KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY 4250
    GGRVDNEFDQ RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR 4300
    EEFVQWVELL PDAQTPSWLG LPNNAERVLL TTQGVDMISK MLKMQMLEDE 4350
    DDLAYAETEK KARTDSTSDG RPAWMRTLHT TASNWLHLIP QTLSPLKRTV 4400
    ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK KQTNYLRTLI 4450
    NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAASGGAK 4500
    ELKNIHVCLG GLFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSAT 4550
    LDACSFGVTG LKLQGATCSN NKLSLSNAIS TVLPLTQLRW VKQTSAEKKA 4600
    SVVTLPVYLN FTRADLIFTV DFEIATKEDP RSFYERGVAV LCTE 4644
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    ProteinModelPortali Q9JHU4.
    SMRi Q9JHU4. Positions 3264-3427.
    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 ENSGT00750000117443.
    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.

    Miscellaneous databases

    ChiTaRSi DYNC1H1. mouse.
    EvolutionaryTracei Q9JHU4.
    NextBioi 283839.
    PROi Q9JHU4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JHU4.
    Bgeei Q9JHU4.
    CleanExi MM_DYNC1H1.
    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

    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: October 1, 2014
    This is version 124 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