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Q14204

- DYHC1_HUMAN

UniProt

Q14204 - DYHC1_HUMAN

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Protein

Cytoplasmic dynein 1 heavy chain 1

Gene
DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325
Organism
Homo sapiens (Human)
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 bindingi1906 – 19138ATP Reviewed prediction
Nucleotide bindingi2224 – 22318ATP Reviewed prediction
Nucleotide bindingi2595 – 26028ATP Reviewed prediction
Nucleotide bindingi2937 – 29448ATP Reviewed prediction

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
Complete GO annotation...

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. microtubule Source: UniProtKB
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.

Binary interactionsi

WithEntry#Exp.IntActNotes
DISC1Q9NRI53EBI-356015,EBI-529989
HTTP428583EBI-356015,EBI-466029
PSEN2P498103EBI-356015,EBI-2010251

Protein-protein interaction databases

BioGridi108117. 104 interactions.
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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 18671815Stem By similarityAdd
BLAST
Regioni448 – 703256Interaction with DYNC1I2 By similarityAdd
BLAST
Regioni651 – 802152Interaction with DYNC1LI2 By similarityAdd
BLAST
Regioni1868 – 2099232AAA 1 By similarityAdd
BLAST
Regioni2180 – 2452273AAA 2 By similarityAdd
BLAST
Regioni2556 – 2805250AAA 3 By similarityAdd
BLAST
Regioni2899 – 3168270AAA 4 By similarityAdd
BLAST
Regioni3189 – 3500312Stalk By similarityAdd
BLAST
Regioni3553 – 3782230AAA 5 By similarityAdd
BLAST
Regioni4005 – 4221217AAA 6 By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili181 – 20222 Reviewed predictionAdd
BLAST
Coiled coili455 – 47824 Reviewed predictionAdd
BLAST
Coiled coili543 – 56624 Reviewed predictionAdd
BLAST
Coiled coili1171 – 125282 Reviewed predictionAdd
BLAST
Coiled coili1357 – 137317 Reviewed predictionAdd
BLAST
Coiled coili3189 – 327587 Reviewed predictionAdd
BLAST
Coiled coili3396 – 3500105 Reviewed predictionAdd
BLAST
Coiled coili3737 – 380064 Reviewed predictionAdd
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.
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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1778 – 17792LH → SD in AAB09727. 1 Publication
Sequence conflicti1941 – 19411M → R in AAB09727. 1 Publication
Sequence conflicti2025 – 20251R → N in AAB09727. 1 Publication

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.
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 146 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

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