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Q9JHU4

- DYHC1_MOUSE

UniProt

Q9JHU4 - DYHC1_MOUSE

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Protein
Cytoplasmic dynein 1 heavy chain 1
Gene
Dync1h1, Dhc1, Dnch1, Dnchc1, Dyhc
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 – 19118ATP Reviewed prediction
Nucleotide bindingi2222 – 22298ATP Reviewed prediction
Nucleotide bindingi2593 – 26008ATP Reviewed prediction
Nucleotide bindingi2935 – 29428ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: InterPro
  3. dynein light intermediate chain binding Source: MGI
  4. microtubule motor activity Source: InterPro
  5. protein binding Source: IntAct
Complete GO annotation...

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.

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. Golgi apparatus Source: Ensembl
  2. axonemal dynein complex Source: MGI
  3. centrosome Source: Ensembl
  4. cytoplasm Source: MGI
  5. extracellular vesicular exosome Source: Ensembl
  6. filopodium Source: MGI
  7. 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.1 Publication
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 – 11Removed By similarity
Chaini2 – 46444643Cytoplasmic dynein 1 heavy chain 1
PRO_0000114628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei1123 – 11231N6-acetyllysine By similarity
Modified residuei3478 – 34781N6-acetyllysine By similarity
Modified residuei4281 – 42811N6-acetyllysine1 Publication
Modified residuei4366 – 43661Phosphoserine By 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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199254. 22 interactions.
IntActiQ9JHU4. 26 interactions.
MINTiMINT-1728570.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9JHU4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 18651864Stem By similarity
Add
BLAST
Regioni446 – 701256Interaction with DYNC1I2 By similarity
Add
BLAST
Regioni649 – 800152Interaction with DYNC1LI2 By similarity
Add
BLAST
Regioni1866 – 2097232AAA 1 By similarity
Add
BLAST
Regioni2178 – 2450273AAA 2 By similarity
Add
BLAST
Regioni2554 – 2803250AAA 3 By similarity
Add
BLAST
Regioni2897 – 3166270AAA 4 By similarity
Add
BLAST
Regioni3187 – 3498312Stalk By similarity
Add
BLAST
Regioni3551 – 3780230AAA 5 By similarity
Add
BLAST
Regioni4003 – 4219217AAA 6 By similarity
Add
BLAST

Coiled coil

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

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

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 conflict

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

Protein-protein interaction databases

BioGridi 199254. 22 interactions.
IntActi Q9JHU4. 26 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

« 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: September 3, 2014
This is version 123 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

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