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Q14204

- DYHC1_HUMAN

UniProt

Q14204 - DYHC1_HUMAN

Protein

Cytoplasmic dynein 1 heavy chain 1

Gene

DYNC1H1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 5 (04 Jan 2005)
      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 bindingi1906 – 19138ATPSequence Analysis
    Nucleotide bindingi2224 – 22318ATPSequence Analysis
    Nucleotide bindingi2595 – 26028ATPSequence Analysis
    Nucleotide bindingi2937 – 29448ATPSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. microtubule motor activity Source: InterPro
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. cell death Source: UniProtKB-KW
    3. cytoplasmic mRNA processing body assembly Source: BHF-UCL
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. microtubule-based movement Source: InterPro
    6. mitotic cell cycle Source: Reactome
    7. mitotic spindle organization Source: UniProtKB
    8. stress granule assembly Source: BHF-UCL
    9. transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Motor protein

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. 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, DNCL, DNECL, DYHC, KIAA0325
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:2961. DYNC1H1.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasmic dynein complex Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProtKB
    5. membrane Source: UniProtKB
    6. microtubule Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Dynein, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 2O (CMT2O) [MIM:614228]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti306 – 3061H → R in CMT2O and SMALED1. 2 Publications
    VAR_066651
    Mental retardation, autosomal dominant 13 (MRD13) [MIM:614563]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD13 is associated with variable neuronal migration defects and mild dysmorphic features. Some patients may also show signs of peripheral neuropathy, such as abnormal gait and hyporeflexia.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291K → I in MRD13. 1 Publication
    VAR_070580
    Natural varianti659 – 6624Missing in MRD13.
    VAR_070581
    Natural varianti1518 – 15181E → K in MRD13. 2 Publications
    VAR_067823
    Natural varianti1567 – 15671R → Q in MRD13. 1 Publication
    VAR_070582
    Natural varianti1962 – 19621R → C in MRD13. 1 Publication
    VAR_070583
    Natural varianti3241 – 32411K → T in MRD13. 1 Publication
    VAR_070584
    Natural varianti3336 – 33361K → N in MRD13; shows a substantial reduction in the microtubule binding affinity compared to the wild-type control protein. 1 Publication
    VAR_070585
    Natural varianti3344 – 33441R → Q in MRD13. 1 Publication
    VAR_070586
    Natural varianti3384 – 33841R → Q in MRD13; shows a substantial reduction in the microtubule binding affinity compared to the wild-type control protein. 1 Publication
    VAR_070587
    Natural varianti3822 – 38221H → P in MRD13; de novo mutation. 1 Publication
    VAR_065085
    Spinal muscular atrophy, lower extremity-predominant 1, autosomal dominant (SMALED1) [MIM:158600]: A form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMALED1 is characterized by muscle weakness predominantly affecting the proximal lower extremities.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti306 – 3061H → R in CMT2O and SMALED1. 2 Publications
    VAR_066651
    Natural varianti584 – 5841I → L in SMALED1; disrupts dynein complex stability and function. 1 Publication
    VAR_067820
    Natural varianti671 – 6711K → E in SMALED1. 1 Publication
    VAR_067821
    Natural varianti970 – 9701Y → C in SMALED1. 1 Publication
    VAR_067822

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Mental retardation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi158600. phenotype.
    614228. phenotype.
    614563. phenotype.
    Orphaneti284232. Autosomal dominant Charcot-Marie-Tooth disease type 2O.
    209341. Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures.
    178469. Autosomal dominant nonsyndromic intellectual disability.
    PharmGKBiPA27432.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 46464645Cytoplasmic dynein 1 heavy chain 1PRO_0000114627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei1125 – 11251N6-acetyllysine1 Publication
    Modified residuei3480 – 34801N6-acetyllysine1 Publication
    Modified residuei4283 – 42831N6-acetyllysine1 Publication
    Modified residuei4368 – 43681Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14204.
    PaxDbiQ14204.
    PRIDEiQ14204.

    PTM databases

    PhosphoSiteiQ14204.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14204.
    BgeeiQ14204.
    CleanExiHS_DYNC1H1.
    GenevestigatoriQ14204.

    Organism-specific databases

    HPAiCAB010443.
    HPA003742.

    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
    DISC1Q9NRI53EBI-356015,EBI-529989
    HTTP428583EBI-356015,EBI-466029
    PSEN2P498103EBI-356015,EBI-2010251

    Protein-protein interaction databases

    BioGridi108117. 104 interactions.
    DIPiDIP-37544N.
    IntActiQ14204. 33 interactions.
    MINTiMINT-5003694.
    STRINGi9606.ENSP00000348965.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BORmodel-A3200-3299[»]
    B3398-3497[»]
    2BOTmodel-A3197-3296[»]
    B3398-3497[»]
    ProteinModelPortaliQ14204.
    SMRiQ14204. Positions 1899-1963, 2215-2243, 2587-2622, 2928-2996, 3266-3429, 4038-4330.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 18671815StemBy similarityAdd
    BLAST
    Regioni448 – 703256Interaction with DYNC1I2By similarityAdd
    BLAST
    Regioni651 – 802152Interaction with DYNC1LI2By similarityAdd
    BLAST
    Regioni1868 – 2099232AAA 1By similarityAdd
    BLAST
    Regioni2180 – 2452273AAA 2By similarityAdd
    BLAST
    Regioni2556 – 2805250AAA 3By similarityAdd
    BLAST
    Regioni2899 – 3168270AAA 4By similarityAdd
    BLAST
    Regioni3189 – 3500312StalkBy similarityAdd
    BLAST
    Regioni3553 – 3782230AAA 5By similarityAdd
    BLAST
    Regioni4005 – 4221217AAA 6By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili181 – 20222Sequence AnalysisAdd
    BLAST
    Coiled coili455 – 47824Sequence AnalysisAdd
    BLAST
    Coiled coili543 – 56624Sequence AnalysisAdd
    BLAST
    Coiled coili1171 – 125282Sequence AnalysisAdd
    BLAST
    Coiled coili1357 – 137317Sequence AnalysisAdd
    BLAST
    Coiled coili3189 – 327587Sequence AnalysisAdd
    BLAST
    Coiled coili3396 – 3500105Sequence AnalysisAdd
    BLAST
    Coiled coili3737 – 380064Sequence 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.
    HOGENOMiHOG000176055.
    HOVERGENiHBG096595.
    InParanoidiQ14204.
    KOiK10413.
    OMAiMQIDQLE.
    OrthoDBiEOG76471R.
    PhylomeDBiQ14204.
    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.

    Q14204-1 [UniParc]FASTAAdd to Basket

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    MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA     50
    ALEAALEEKS ALEQMRKFLS DPQVHTVLVE RSTLKEDVGD EGEEEKEFIS 100
    YNINIDIHYG VKSNSLAFIK RTPVIDADKP VSSQLRVLTL SEDSPYETLH 150
    SFISNAVAPF FKSYIRESGK ADRDGDKMAP SVEKKIAELE MGLLHLQQNI 200
    EIPEISLPIH PMITNVAKQC YERGEKPKVT DFGDKVEDPT FLNQLQSGVN 250
    RWIREIQKVT KLDRDPASGT ALQEISFWLN LERALYRIQE KRESPEVLLT 300
    LDILKHGKRF HATVSFDTDT GLKQALETVN DYNPLMKDFP LNDLLSATEL 350
    DKIRQALVAI FTHLRKIRNT KYPIQRALRL VEAISRDLSS QLLKVLGTRK 400
    LMHVAYEEFE KVMVACFEVF QTWDDEYEKL QVLLRDIVKR KREENLKMVW 450
    RINPAHRKLQ ARLDQMRKFR RQHEQLRAVI VRVLRPQVTA VAQQNQGEVP 500
    EPQDMKVAEV LFDAADANAI EEVNLAYENV KEVDGLDVSK EGTEAWEAAM 550
    KRYDERIDRV ETRITARLRD QLGTAKNANE MFRIFSRFNA LFVRPHIRGA 600
    IREYQTQLIQ RVKDDIESLH DKFKVQYPQS QACKMSHVRD LPPVSGSIIW 650
    AKQIDRQLTA YMKRVEDVLG KGWENHVEGQ KLKQDGDSFR MKLNTQEIFD 700
    DWARKVQQRN LGVSGRIFTI ESTRVRGRTG NVLKLKVNFL PEIITLSKEV 750
    RNLKWLGFRV PLAIVNKAHQ ANQLYPFAIS LIESVRTYER TCEKVEERNT 800
    ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV FNFQEKVDDL 850
    LIIEEKIDLE VRSLETCMYD HKTFSEILNR VQKAVDDLNL HSYSNLPIWV 900
    NKLDMEIERI LGVRLQAGLR AWTQVLLGQA EDKAEVDMDT DAPQVSHKPG 950
    GEPKIKNVVH ELRITNQVIY LNPPIEECRY KLYQEMFAWK MVVLSLPRIQ 1000
    SQRYQVGVHY ELTEEEKFYR NALTRMPDGP VALEESYSAV MGIVSEVEQY 1050
    VKVWLQYQCL WDMQAENIYN RLGEDLNKWQ ALLVQIRKAR GTFDNAETKK 1100
    EFGPVVIDYG KVQSKVNLKY DSWHKEVLSK FGQMLGSNMT EFHSQISKSR 1150
    QELEQHSVDT ASTSDAVTFI TYVQSLKRKI KQFEKQVELY RNGQRLLEKQ 1200
    RFQFPPSWLY IDNIEGEWGA FNDIMRRKDS AIQQQVANLQ MKIVQEDRAV 1250
    ESRTTDLLTD WEKTKPVTGN LRPEEALQAL TIYEGKFGRL KDDREKCAKA 1300
    KEALELTDTG LLSGSEERVQ VALEELQDLK GVWSELSKVW EQIDQMKEQP 1350
    WVSVQPRKLR QNLDALLNQL KSFPARLRQY ASYEFVQRLL KGYMKINMLV 1400
    IELKSEALKD RHWKQLMKRL HVNWVVSELT LGQIWDVDLQ KNEAIVKDVL 1450
    LVAQGEMALE EFLKQIREVW NTYELDLVNY QNKCRLIRGW DDLFNKVKEH 1500
    INSVSAMKLS PYYKVFEEDA LSWEDKLNRI MALFDVWIDV QRRWVYLEGI 1550
    FTGSADIKHL LPVETQRFQS ISTEFLALMK KVSKSPLVMD VLNIQGVQRS 1600
    LERLADLLGK IQKALGEYLE RERSSFPRFY FVGDEDLLEI IGNSKNVAKL 1650
    QKHFKKMFAG VSSIILNEDN SVVLGISSRE GEEVMFKTPV SITEHPKINE 1700
    WLTLVEKEMR VTLAKLLAES VTEVEIFGKA TSIDPNTYIT WIDKYQAQLV 1750
    VLSAQIAWSE NVETALSSMG GGGDAAPLHS VLSNVEVTLN VLADSVLMEQ 1800
    PPLRRRKLEH LITELVHQRD VTRSLIKSKI DNAKSFEWLS QMRFYFDPKQ 1850
    TDVLQQLSIQ MANAKFNYGF EYLGVQDKLV QTPLTDRCYL TMTQALEARL 1900
    GGSPFGPAGT GKTESVKALG HQLGRFVLVF NCDETFDFQA MGRIFVGLCQ 1950
    VGAWGCFDEF NRLEERMLSA VSQQVQCIQE ALREHSNPNY DKTSAPITCE 2000
    LLNKQVKVSP DMAIFITMNP GYAGRSNLPD NLKKLFRSLA MTKPDRQLIA 2050
    QVMLYSQGFR TAEVLANKIV PFFKLCDEQL SSQSHYDFGL RALKSVLVSA 2100
    GNVKRERIQK IKREKEERGE AVDEGEIAEN LPEQEILIQS VCETMVPKLV 2150
    AEDIPLLFSL LSDVFPGVQY HRGEMTALRE ELKKVCQEMY LTYGDGEEVG 2200
    GMWVEKVLQL YQITQINHGL MMVGPSGSGK SMAWRVLLKA LERLEGVEGV 2250
    AHIIDPKAIS KDHLYGTLDP NTREWTDGLF THVLRKIIDS VRGELQKRQW 2300
    IVFDGDVDPE WVENLNSVLD DNKLLTLPNG ERLSLPPNVR IMFEVQDLKY 2350
    ATLATVSRCG MVWFSEDVLS TDMIFNNFLA RLRSIPLDEG EDEAQRRRKG 2400
    KEDEGEEAAS PMLQIQRDAA TIMQPYFTSN GLVTKALEHA FQLEHIMDLT 2450
    RLRCLGSLFS MLHQACRNVA QYNANHPDFP MQIEQLERYI QRYLVYAILW 2500
    SLSGDSRLKM RAELGEYIRR ITTVPLPTAP NIPIIDYEVS ISGEWSPWQA 2550
    KVPQIEVETH KVAAPDVVVP TLDTVRHEAL LYTWLAEHKP LVLCGPPGSG 2600
    KTMTLFSALR ALPDMEVVGL NFSSATTPEL LLKTFDHYCE YRRTPNGVVL 2650
    APVQLGKWLV LFCDEINLPD MDKYGTQRVI SFIRQMVEHG GFYRTSDQTW 2700
    VKLERIQFVG ACNPPTDPGR KPLSHRFLRH VPVVYVDYPG PASLTQIYGT 2750
    FNRAMLRLIP SLRTYAEPLT AAMVEFYTMS QERFTQDTQP HYIYSPREMT 2800
    RWVRGIFEAL RPLETLPVEG LIRIWAHEAL RLFQDRLVED EERRWTDENI 2850
    DTVALKHFPN IDREKAMSRP ILYSNWLSKD YIPVDQEELR DYVKARLKVF 2900
    YEEELDVPLV LFNEVLDHVL RIDRIFRQPQ GHLLLIGVSG AGKTTLSRFV 2950
    AWMNGLSVYQ IKVHRKYTGE DFDEDLRTVL RRSGCKNEKI AFIMDESNVL 3000
    DSGFLERMNT LLANGEVPGL FEGDEYATLM TQCKEGAQKE GLMLDSHEEL 3050
    YKWFTSQVIR NLHVVFTMNP SSEGLKDRAA TSPALFNRCV LNWFGDWSTE 3100
    ALYQVGKEFT SKMDLEKPNY IVPDYMPVVY DKLPQPPSHR EAIVNSCVFV 3150
    HQTLHQANAR LAKRGGRTMA ITPRHYLDFI NHYANLFHEK RSELEEQQMH 3200
    LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL KKMVKDQQEA 3250
    EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAVI EAQNAVKSIK 3300
    KQHLVEVRSM ANPPAAVKLA LESICLLLGE STTDWKQIRS IIMRENFIPT 3350
    IVNFSAEEIS DAIREKMKKN YMSNPSYNYE IVNRASLACG PMVKWAIAQL 3400
    NYADMLKRVE PLRNELQKLE DDAKDNQQKA NEVEQMIRDL EASIARYKEE 3450
    YAVLISEAQA IKADLAAVEA KVNRSTALLK SLSAERERWE KTSETFKNQM 3500
    STIAGDCLLS AAFIAYAGYF DQQMRQNLFT TWSHHLQQAN IQFRTDIART 3550
    EYLSNADERL RWQASSLPAD DLCTENAIML KRFNRYPLII DPSGQATEFI 3600
    MNEYKDRKIT RTSFLDDAFR KNLESALRFG NPLLVQDVES YDPVLNPVLN 3650
    REVRRTGGRV LITLGDQDID LSPSFVIFLS TRDPTVEFPP DLCSRVTFVN 3700
    FTVTRSSLQS QCLNEVLKAE RPDVDEKRSD LLKLQGEFQL RLRQLEKSLL 3750
    QALNEVKGRI LDDDTIITTL ENLKREAAEV TRKVEETDIV MQEVETVSQQ 3800
    YLPLSTACSS IYFTMESLKQ IHFLYQYSLQ FFLDIYHNVL YENPNLKGVT 3850
    DHTQRLSIIT KDLFQVAFNR VARGMLHQDH ITFAMLLARI KLKGTVGEPT 3900
    YDAEFQHFLR GNEIVLSAGS TPRIQGLTVE QAEAVVRLSC LPAFKDLIAK 3950
    VQADEQFGIW LDSSSPEQTV PYLWSEETPA TPIGQAIHRL LLIQAFRPDR 4000
    LLAMAHMFVS TNLGESFMSI MEQPLDLTHI VGTEVKPNTP VLMCSVPGYD 4050
    ASGHVEDLAA EQNTQITSIA IGSAEGFNQA DKAINTAVKS GRWVMLKNVH 4100
    LAPGWLMQLE KKLHSLQPHA CFRLFLTMEI NPKVPVNLLR AGRIFVFEPP 4150
    PGVKANMLRT FSSIPVSRIC KSPNERARLY FLLAWFHAII QERLRYAPLG 4200
    WSKKYEFGES DLRSACDTVD TWLDDTAKGR QNISPDKIPW SALKTLMAQS 4250
    IYGGRVDNEF DQRLLNTFLE RLFTTRSFDS EFKLACKVDG HKDIQMPDGI 4300
    RREEFVQWVE LLPDTQTPSW LGLPNNAERV LLTTQGVDMI SKMLKMQMLE 4350
    DEDDLAYAET EKKTRTDSTS DGRPAWMRTL HTTASNWLHL IPQTLSHLKR 4400
    TVENIKDPLF RFFEREVKMG AKLLQDVRQD LADVVQVCEG KKKQTNYLRT 4450
    LINELVKGIL PRSWSHYTVP AGMTVIQWVS DFSERIKQLQ NISLAAASGG 4500
    AKELKNIHVC LGGLFVPEAY ITATRQYVAQ ANSWSLEELC LEVNVTTSQG 4550
    ATLDACSFGV TGLKLQGATC NNNKLSLSNA ISTALPLTQL RWVKQTNTEK 4600
    KASVVTLPVY LNFTRADLIF TVDFEIATKE DPRSFYERGV AVLCTE 4646
    Length:4,646
    Mass (Da):532,408
    Last modified:January 4, 2005 - v5
    Checksum:iD4D4E15DFBDE4797
    GO

    Sequence cautioni

    The sequence BAA20783.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1778 – 17792LH → SD in AAB09727. (PubMed:8666668)Curated
    Sequence conflicti1941 – 19411M → R in AAB09727. (PubMed:8666668)Curated
    Sequence conflicti2025 – 20251R → N in AAB09727. (PubMed:8666668)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291K → I in MRD13. 1 Publication
    VAR_070580
    Natural varianti142 – 1421E → A.1 Publication
    VAR_069437
    Natural varianti306 – 3061H → R in CMT2O and SMALED1. 2 Publications
    VAR_066651
    Natural varianti584 – 5841I → L in SMALED1; disrupts dynein complex stability and function. 1 Publication
    VAR_067820
    Natural varianti659 – 6624Missing in MRD13.
    VAR_070581
    Natural varianti671 – 6711K → E in SMALED1. 1 Publication
    VAR_067821
    Natural varianti970 – 9701Y → C in SMALED1. 1 Publication
    VAR_067822
    Natural varianti1250 – 12501V → L.1 Publication
    VAR_069438
    Natural varianti1518 – 15181E → K in MRD13. 2 Publications
    VAR_067823
    Natural varianti1567 – 15671R → Q in MRD13. 1 Publication
    VAR_070582
    Natural varianti1962 – 19621R → C in MRD13. 1 Publication
    VAR_070583
    Natural varianti2247 – 22471V → M.1 Publication
    VAR_069439
    Natural varianti3241 – 32411K → T in MRD13. 1 Publication
    VAR_070584
    Natural varianti3336 – 33361K → N in MRD13; shows a substantial reduction in the microtubule binding affinity compared to the wild-type control protein. 1 Publication
    VAR_070585
    Natural varianti3344 – 33441R → Q in MRD13. 1 Publication
    VAR_070586
    Natural varianti3384 – 33841R → Q in MRD13; shows a substantial reduction in the microtubule binding affinity compared to the wild-type control protein. 1 Publication
    VAR_070587
    Natural varianti3822 – 38221H → P in MRD13; de novo mutation. 1 Publication
    VAR_065085
    Natural varianti3902 – 39021D → N.1 Publication
    Corresponds to variant rs17512818 [ dbSNP | Ensembl ].
    VAR_020889
    Natural varianti4029 – 40291H → Q.2 Publications
    Corresponds to variant rs10129889 [ dbSNP | Ensembl ].
    VAR_020890
    Natural varianti4143 – 41431R → C.1 Publication
    VAR_069440
    Natural varianti4285 – 42851A → S.1 Publication
    VAR_069441
    Natural varianti4421 – 44211A → T.1 Publication
    VAR_069442
    Natural varianti4507 – 45071I → S.1 Publication
    VAR_069443
    Natural varianti4603 – 46031S → G.1 Publication
    VAR_069444

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002323 mRNA. Translation: BAA20783.3. Different initiation.
    AB290157 mRNA. Translation: BAG06711.1.
    AY682080 Genomic DNA. Translation: AAT74625.1.
    U53530 mRNA. Translation: AAB09727.1.
    L23958 mRNA. Translation: AAA16065.1.
    BC021297 mRNA. Translation: AAH21297.2.
    CCDSiCCDS9966.1.
    PIRiA49019.
    G02529.
    RefSeqiNP_001367.2. NM_001376.4.
    UniGeneiHs.614080.

    Genome annotation databases

    EnsembliENST00000360184; ENSP00000348965; ENSG00000197102.
    GeneIDi1778.
    KEGGihsa:1778.
    UCSCiuc001yks.2. human.

    Polymorphism databases

    DMDMi57015308.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB002323 mRNA. Translation: BAA20783.3 . Different initiation.
    AB290157 mRNA. Translation: BAG06711.1 .
    AY682080 Genomic DNA. Translation: AAT74625.1 .
    U53530 mRNA. Translation: AAB09727.1 .
    L23958 mRNA. Translation: AAA16065.1 .
    BC021297 mRNA. Translation: AAH21297.2 .
    CCDSi CCDS9966.1.
    PIRi A49019.
    G02529.
    RefSeqi NP_001367.2. NM_001376.4.
    UniGenei Hs.614080.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BOR model - A 3200-3299 [» ]
    B 3398-3497 [» ]
    2BOT model - A 3197-3296 [» ]
    B 3398-3497 [» ]
    ProteinModelPortali Q14204.
    SMRi Q14204. Positions 1899-1963, 2215-2243, 2587-2622, 2928-2996, 3266-3429, 4038-4330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108117. 104 interactions.
    DIPi DIP-37544N.
    IntActi Q14204. 33 interactions.
    MINTi MINT-5003694.
    STRINGi 9606.ENSP00000348965.

    PTM databases

    PhosphoSitei Q14204.

    Polymorphism databases

    DMDMi 57015308.

    Proteomic databases

    MaxQBi Q14204.
    PaxDbi Q14204.
    PRIDEi Q14204.

    Protocols and materials databases

    DNASUi 1778.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360184 ; ENSP00000348965 ; ENSG00000197102 .
    GeneIDi 1778.
    KEGGi hsa:1778.
    UCSCi uc001yks.2. human.

    Organism-specific databases

    CTDi 1778.
    GeneCardsi GC14P102430.
    GeneReviewsi DYNC1H1.
    HGNCi HGNC:2961. DYNC1H1.
    HPAi CAB010443.
    HPA003742.
    MIMi 158600. phenotype.
    600112. gene.
    614228. phenotype.
    614563. phenotype.
    neXtProti NX_Q14204.
    Orphaneti 284232. Autosomal dominant Charcot-Marie-Tooth disease type 2O.
    209341. Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures.
    178469. Autosomal dominant nonsyndromic intellectual disability.
    PharmGKBi PA27432.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5245.
    HOGENOMi HOG000176055.
    HOVERGENi HBG096595.
    InParanoidi Q14204.
    KOi K10413.
    OMAi MQIDQLE.
    OrthoDBi EOG76471R.
    PhylomeDBi Q14204.
    TreeFami TF101165.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    ChiTaRSi DYNC1H1. human.
    GeneWikii DYNC1H1.
    GenomeRNAii 1778.
    NextBioi 7239.
    PROi Q14204.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14204.
    Bgeei Q14204.
    CleanExi HS_DYNC1H1.
    Genevestigatori Q14204.

    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. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-4029.
      Tissue: Brain.
    2. Ohara O., Nagase T., Kikuno R., Yamakawa H., Nomura N.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free recombination: preparation of full-length cDNA clones encoding motor proteins."
      Yamakawa H., Kikuno R.F., Nagase T., Ohara O.
      Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. NIEHS SNPs program
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-3902 AND GLN-4029.
    5. "Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles."
      Vaisberg E.A., Grissom P.M., McIntosh J.R.
      J. Cell Biol. 133:831-842(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1130-2026.
    6. "Cytoplasmic dynein plays a role in mammalian mitotic spindle formation."
      Vaisberg E.A., Koonce M.P., McIntosh J.R.
      J. Cell Biol. 123:849-858(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1884-2024.
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3658-4646.
      Tissue: Placenta.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1125; LYS-3480 AND LYS-4283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. Cited for: VARIANT MRD13 PRO-3822.
    16. "Exome sequencing identifies a DYNC1H1 mutation in a large pedigree with dominant axonal Charcot-Marie-Tooth disease."
      Weedon M.N., Hastings R., Caswell R., Xie W., Paszkiewicz K., Antoniadi T., Williams M., King C., Greenhalgh L., Newbury-Ecob R., Ellard S.
      Am. J. Hum. Genet. 89:308-312(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2O ARG-306.
    17. Cited for: VARIANT MRD13 LYS-1518.
    18. "A DYNC1H1 mutation causes a dominant spinal muscular atrophy with lower extremity predominance."
      Tsurusaki Y., Saitoh S., Tomizawa K., Sudo A., Asahina N., Shiraishi H., Ito J.I., Tanaka H., Doi H., Saitsu H., Miyake N., Matsumoto N.
      Neurogenetics 13:327-332(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SMALED1 ARG-306.
    19. Cited for: VARIANTS SMALED1 LEU-584; GLU-671 AND CYS-970, CHARACTERIZATION OF VARIANT SMALED1 LEU-584.
    20. Cited for: VARIANT MRD13 LYS-1518, VARIANTS ALA-142; LEU-1250; MET-2247; CYS-4143; SER-4285; THR-4421; SER-4507 AND GLY-4603.
    21. Cited for: VARIANTS MRD13 ILE-129; 659-THR--MET-662 DEL; GLN-1567; CYS-1962; THR-3241; ASN-3336; GLN-3344 AND GLN-3384, CHARACTERIZATION OF VARIANTS MRD13 ASN-3336 AND GLN-3384.

    Entry informationi

    Entry nameiDYHC1_HUMAN
    AccessioniPrimary (citable) accession number: Q14204
    Secondary accession number(s): B0I1R0
    , Q6DKQ7, Q8WU28, Q92814, Q9Y4G5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 147 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3