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P38650

- DYHC1_RAT

UniProt

P38650 - DYHC1_RAT

Protein

Cytoplasmic dynein 1 heavy chain 1

Gene

Dync1h1

Organism
Rattus norvegicus (Rat)
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 1 (01 Feb 1995)
      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. microtubule motor activity Source: InterPro
    4. protein binding Source: HGNC

    GO - Biological processi

    1. microtubule-based movement Source: InterPro
    2. transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Motor protein

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytoplasmic dynein 1 heavy chain 1
    Alternative name(s):
    Cytoplasmic dynein heavy chain 1
    Dynein heavy chain, cytosolic
    MAP 1C
    Gene namesi
    Name:Dync1h1
    Synonyms:Dhc1, Dnch1, Dnchc1, Dnec1, Dyhc, Map1c
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2511. Dync1h1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. dynein complex Source: UniProtKB-KW
    3. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Dynein, Microtubule

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 46444643Cytoplasmic dynein 1 heavy chain 1PRO_0000114629Add
    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-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP38650.
    PRIDEiP38650.

    Expressioni

    Gene expression databases

    GenevestigatoriP38650.

    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 DYNC1I2.2 Publications

    Protein-protein interaction databases

    BioGridi248131. 6 interactions.
    IntActiP38650. 4 interactions.
    MINTiMINT-4564742.

    Structurei

    3D structure databases

    ProteinModelPortaliP38650.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 18651864StemBy similarityAdd
    BLAST
    Regioni446 – 701256Interaction with DYNC1I2Add
    BLAST
    Regioni649 – 800152Interaction with DYNC1LI2Add
    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.
    HOGENOMiHOG000176055.
    HOVERGENiHBG096595.
    InParanoidiP38650.
    KOiK10413.
    PhylomeDBiP38650.

    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.

    P38650-1 [UniParc]FASTAAdd to Basket

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    MSETGGGEDG SAGLEVSAVQ NVADVSVLQK 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 ARVRGRSGNV 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 YQEMFAWKMI VLSLPRIQSQ 1000
    RYQVGVHYEL TEEEKFYRNA LTRSRDGPVA LEESYSAVMG IVTEVEQYVK 1050
    VWLQYQCLWD MQAENIYNRL GEDLSKWQAL LVQIRRARGT 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 EAIVKDVLLV 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 SIILNEDSSV VLGISSREGE EVMFKTPVSI TEHPKINEWL 1700
    TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI DKYQAQLVVL 1750
    SAQIAWSENV ENALSNVGGG GNVGPLQSVL 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 LKSVLVSPGN 2100
    VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSFC ETMVPKLVAE 2150
    DIPLLFSLLS DVFPGVQYHR GEMTDLREEL KKVCKEMYLT YGDGEEVGGM 2200
    WVEKVLQLYQ ITQINHGLMM VGPSGSGKSM AWRVLLKALE RLEGVEGVAH 2250
    IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDNVR GELQKRQWIV 2300
    FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM FEVQDLKYAT 2350
    LATVSRCGMV WFSEDLLSTD MIFNNFLARL RTIPLDEGED EAQRRRKGKE 2400
    DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL 2450
    RCLGSLFSML HQGCRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL 2500
    SGDSRLKMRA ELGEYIRRIT TVPLPTAPNI 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 DQVEELRRAL 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
    TQRLSVITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTMGEPTYD 3900
    AEFQHFLRGK EIVLSAGSTP KVQGLTVEQA EAVARLSCLP AFKDLIAKVQ 3950
    ADEQFGIWLE SSSPEQTVPY LWTEETPATP IGQAIHRLLL IQAFRPDRLL 4000
    AMAHMFVSTN LGESFMSIME QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS 4050
    GHVEDLAAEQ NTQITSIAIG SAEGFNQADK AINTAVKSGR WVMLKNVHLA 4100
    PGWLMQLEKK LHSLQPHACF RLFLTMEINP RVPVNLLRAG RIFVFEPPPG 4150
    VKANMLRTFS SIPVSRMCKS PNERARLYFL LAWFHAVIQE RLRYAPLGWS 4200
    KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY 4250
    GGRVDNEFDQ RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR 4300
    EEFVQWVELL PDAQTPSWLG LPNNAERVLL TTQGVDMISK MLKMQMLEDE 4350
    DDLAYAETEK KTRTDFTSDG RPAWMRTLHT TASNWLHLIP QTLSPLKRTV 4400
    ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK KQTNYLRTLI 4450
    NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAAAGGAK 4500
    ELKNIHVCLG ALFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSTT 4550
    LDACSFGVTG LKLQGATCSN NKLSLSNAIS TVLPLTQLRW GKQTSAEKKA 4600
    SVVTLPVYLN FTRADLIFTV DFEIATKEDP RSFYERGVAV LCTE 4644
    Length:4,644
    Mass (Da):532,252
    Last modified:February 1, 1995 - v1
    Checksum:i8C6ABDBEDF875D82
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1024 – 10252SR → MP in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti1772 – 17721N → D in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti2098 – 20981P → A in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti2139 – 21391F → V in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti2175 – 21751D → A in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti2185 – 21851K → Q in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti2366 – 23661L → V in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti2382 – 23821T → S in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti2463 – 24631G → A in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti3219 – 32191A → D in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti4131 – 41311R → K in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti4366 – 43661F → S in AAA41103. (PubMed:7684232)Curated
    Sequence conflicti4511 – 45111A → G in AAA41103. (PubMed:7684232)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13896 mRNA. Translation: BAA02996.1.
    L08505 mRNA. Translation: AAA41103.1.
    PIRiA38905.
    RefSeqiNP_062099.3. NM_019226.3.
    UniGeneiRn.11027.

    Genome annotation databases

    GeneIDi29489.
    KEGGirno:29489.
    UCSCiRGD:2511. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13896 mRNA. Translation: BAA02996.1 .
    L08505 mRNA. Translation: AAA41103.1 .
    PIRi A38905.
    RefSeqi NP_062099.3. NM_019226.3.
    UniGenei Rn.11027.

    3D structure databases

    ProteinModelPortali P38650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248131. 6 interactions.
    IntActi P38650. 4 interactions.
    MINTi MINT-4564742.

    Chemistry

    BindingDBi P38650.
    ChEMBLi CHEMBL3694.

    Proteomic databases

    PaxDbi P38650.
    PRIDEi P38650.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29489.
    KEGGi rno:29489.
    UCSCi RGD:2511. rat.

    Organism-specific databases

    CTDi 1778.
    RGDi 2511. Dync1h1.

    Phylogenomic databases

    eggNOGi COG5245.
    HOGENOMi HOG000176055.
    HOVERGENi HBG096595.
    InParanoidi P38650.
    KOi K10413.
    PhylomeDBi P38650.

    Miscellaneous databases

    NextBioi 609363.
    PROi P38650.

    Gene expression databases

    Genevestigatori P38650.

    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. "The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme."
      Zhang Z., Tanaka Y., Nonaka S., Aizawa H., Kawasaki H., Nakata T., Hirokawa N.
      Proc. Natl. Acad. Sci. U.S.A. 90:7928-7932(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Brain.
    2. "Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP 1C)."
      Mikami A., Paschal B.M., Mazumdar M., Vallee R.B.
      Neuron 10:787-796(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.
    3. "HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits."
      Neely M.D., Erickson H.P., Boekelheide K.
      J. Biol. Chem. 265:8691-8698(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    4. "Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding."
      Tynan S.H., Gee M.A., Vallee R.B.
      J. Biol. Chem. 275:32769-32774(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DYNC1LI1; DYNC1LI2 AND DYNC1I2.

    Entry informationi

    Entry nameiDYHC1_RAT
    AccessioniPrimary (citable) accession number: P38650
    Secondary accession number(s): Q63178
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3