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Q14204

- DYHC1_HUMAN

UniProt

Q14204 - DYHC1_HUMAN

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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

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

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. filopodium Source: Ensembl
  6. membrane Source: UniProtKB
  7. 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.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. 1 Publication
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 non-syndromic 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

BgeeiQ14204.
CleanExiHS_DYNC1H1.
ExpressionAtlasiQ14204. baseline and differential.
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. 109 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 2215-2243, 2587-2622, 3266-3429, 3471-3840, 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.
GeneTreeiENSGT00760000118964.
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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        10         20         30         40         50
MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA
60 70 80 90 100
ALEAALEEKS ALEQMRKFLS DPQVHTVLVE RSTLKEDVGD EGEEEKEFIS
110 120 130 140 150
YNINIDIHYG VKSNSLAFIK RTPVIDADKP VSSQLRVLTL SEDSPYETLH
160 170 180 190 200
SFISNAVAPF FKSYIRESGK ADRDGDKMAP SVEKKIAELE MGLLHLQQNI
210 220 230 240 250
EIPEISLPIH PMITNVAKQC YERGEKPKVT DFGDKVEDPT FLNQLQSGVN
260 270 280 290 300
RWIREIQKVT KLDRDPASGT ALQEISFWLN LERALYRIQE KRESPEVLLT
310 320 330 340 350
LDILKHGKRF HATVSFDTDT GLKQALETVN DYNPLMKDFP LNDLLSATEL
360 370 380 390 400
DKIRQALVAI FTHLRKIRNT KYPIQRALRL VEAISRDLSS QLLKVLGTRK
410 420 430 440 450
LMHVAYEEFE KVMVACFEVF QTWDDEYEKL QVLLRDIVKR KREENLKMVW
460 470 480 490 500
RINPAHRKLQ ARLDQMRKFR RQHEQLRAVI VRVLRPQVTA VAQQNQGEVP
510 520 530 540 550
EPQDMKVAEV LFDAADANAI EEVNLAYENV KEVDGLDVSK EGTEAWEAAM
560 570 580 590 600
KRYDERIDRV ETRITARLRD QLGTAKNANE MFRIFSRFNA LFVRPHIRGA
610 620 630 640 650
IREYQTQLIQ RVKDDIESLH DKFKVQYPQS QACKMSHVRD LPPVSGSIIW
660 670 680 690 700
AKQIDRQLTA YMKRVEDVLG KGWENHVEGQ KLKQDGDSFR MKLNTQEIFD
710 720 730 740 750
DWARKVQQRN LGVSGRIFTI ESTRVRGRTG NVLKLKVNFL PEIITLSKEV
760 770 780 790 800
RNLKWLGFRV PLAIVNKAHQ ANQLYPFAIS LIESVRTYER TCEKVEERNT
810 820 830 840 850
ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV FNFQEKVDDL
860 870 880 890 900
LIIEEKIDLE VRSLETCMYD HKTFSEILNR VQKAVDDLNL HSYSNLPIWV
910 920 930 940 950
NKLDMEIERI LGVRLQAGLR AWTQVLLGQA EDKAEVDMDT DAPQVSHKPG
960 970 980 990 1000
GEPKIKNVVH ELRITNQVIY LNPPIEECRY KLYQEMFAWK MVVLSLPRIQ
1010 1020 1030 1040 1050
SQRYQVGVHY ELTEEEKFYR NALTRMPDGP VALEESYSAV MGIVSEVEQY
1060 1070 1080 1090 1100
VKVWLQYQCL WDMQAENIYN RLGEDLNKWQ ALLVQIRKAR GTFDNAETKK
1110 1120 1130 1140 1150
EFGPVVIDYG KVQSKVNLKY DSWHKEVLSK FGQMLGSNMT EFHSQISKSR
1160 1170 1180 1190 1200
QELEQHSVDT ASTSDAVTFI TYVQSLKRKI KQFEKQVELY RNGQRLLEKQ
1210 1220 1230 1240 1250
RFQFPPSWLY IDNIEGEWGA FNDIMRRKDS AIQQQVANLQ MKIVQEDRAV
1260 1270 1280 1290 1300
ESRTTDLLTD WEKTKPVTGN LRPEEALQAL TIYEGKFGRL KDDREKCAKA
1310 1320 1330 1340 1350
KEALELTDTG LLSGSEERVQ VALEELQDLK GVWSELSKVW EQIDQMKEQP
1360 1370 1380 1390 1400
WVSVQPRKLR QNLDALLNQL KSFPARLRQY ASYEFVQRLL KGYMKINMLV
1410 1420 1430 1440 1450
IELKSEALKD RHWKQLMKRL HVNWVVSELT LGQIWDVDLQ KNEAIVKDVL
1460 1470 1480 1490 1500
LVAQGEMALE EFLKQIREVW NTYELDLVNY QNKCRLIRGW DDLFNKVKEH
1510 1520 1530 1540 1550
INSVSAMKLS PYYKVFEEDA LSWEDKLNRI MALFDVWIDV QRRWVYLEGI
1560 1570 1580 1590 1600
FTGSADIKHL LPVETQRFQS ISTEFLALMK KVSKSPLVMD VLNIQGVQRS
1610 1620 1630 1640 1650
LERLADLLGK IQKALGEYLE RERSSFPRFY FVGDEDLLEI IGNSKNVAKL
1660 1670 1680 1690 1700
QKHFKKMFAG VSSIILNEDN SVVLGISSRE GEEVMFKTPV SITEHPKINE
1710 1720 1730 1740 1750
WLTLVEKEMR VTLAKLLAES VTEVEIFGKA TSIDPNTYIT WIDKYQAQLV
1760 1770 1780 1790 1800
VLSAQIAWSE NVETALSSMG GGGDAAPLHS VLSNVEVTLN VLADSVLMEQ
1810 1820 1830 1840 1850
PPLRRRKLEH LITELVHQRD VTRSLIKSKI DNAKSFEWLS QMRFYFDPKQ
1860 1870 1880 1890 1900
TDVLQQLSIQ MANAKFNYGF EYLGVQDKLV QTPLTDRCYL TMTQALEARL
1910 1920 1930 1940 1950
GGSPFGPAGT GKTESVKALG HQLGRFVLVF NCDETFDFQA MGRIFVGLCQ
1960 1970 1980 1990 2000
VGAWGCFDEF NRLEERMLSA VSQQVQCIQE ALREHSNPNY DKTSAPITCE
2010 2020 2030 2040 2050
LLNKQVKVSP DMAIFITMNP GYAGRSNLPD NLKKLFRSLA MTKPDRQLIA
2060 2070 2080 2090 2100
QVMLYSQGFR TAEVLANKIV PFFKLCDEQL SSQSHYDFGL RALKSVLVSA
2110 2120 2130 2140 2150
GNVKRERIQK IKREKEERGE AVDEGEIAEN LPEQEILIQS VCETMVPKLV
2160 2170 2180 2190 2200
AEDIPLLFSL LSDVFPGVQY HRGEMTALRE ELKKVCQEMY LTYGDGEEVG
2210 2220 2230 2240 2250
GMWVEKVLQL YQITQINHGL MMVGPSGSGK SMAWRVLLKA LERLEGVEGV
2260 2270 2280 2290 2300
AHIIDPKAIS KDHLYGTLDP NTREWTDGLF THVLRKIIDS VRGELQKRQW
2310 2320 2330 2340 2350
IVFDGDVDPE WVENLNSVLD DNKLLTLPNG ERLSLPPNVR IMFEVQDLKY
2360 2370 2380 2390 2400
ATLATVSRCG MVWFSEDVLS TDMIFNNFLA RLRSIPLDEG EDEAQRRRKG
2410 2420 2430 2440 2450
KEDEGEEAAS PMLQIQRDAA TIMQPYFTSN GLVTKALEHA FQLEHIMDLT
2460 2470 2480 2490 2500
RLRCLGSLFS MLHQACRNVA QYNANHPDFP MQIEQLERYI QRYLVYAILW
2510 2520 2530 2540 2550
SLSGDSRLKM RAELGEYIRR ITTVPLPTAP NIPIIDYEVS ISGEWSPWQA
2560 2570 2580 2590 2600
KVPQIEVETH KVAAPDVVVP TLDTVRHEAL LYTWLAEHKP LVLCGPPGSG
2610 2620 2630 2640 2650
KTMTLFSALR ALPDMEVVGL NFSSATTPEL LLKTFDHYCE YRRTPNGVVL
2660 2670 2680 2690 2700
APVQLGKWLV LFCDEINLPD MDKYGTQRVI SFIRQMVEHG GFYRTSDQTW
2710 2720 2730 2740 2750
VKLERIQFVG ACNPPTDPGR KPLSHRFLRH VPVVYVDYPG PASLTQIYGT
2760 2770 2780 2790 2800
FNRAMLRLIP SLRTYAEPLT AAMVEFYTMS QERFTQDTQP HYIYSPREMT
2810 2820 2830 2840 2850
RWVRGIFEAL RPLETLPVEG LIRIWAHEAL RLFQDRLVED EERRWTDENI
2860 2870 2880 2890 2900
DTVALKHFPN IDREKAMSRP ILYSNWLSKD YIPVDQEELR DYVKARLKVF
2910 2920 2930 2940 2950
YEEELDVPLV LFNEVLDHVL RIDRIFRQPQ GHLLLIGVSG AGKTTLSRFV
2960 2970 2980 2990 3000
AWMNGLSVYQ IKVHRKYTGE DFDEDLRTVL RRSGCKNEKI AFIMDESNVL
3010 3020 3030 3040 3050
DSGFLERMNT LLANGEVPGL FEGDEYATLM TQCKEGAQKE GLMLDSHEEL
3060 3070 3080 3090 3100
YKWFTSQVIR NLHVVFTMNP SSEGLKDRAA TSPALFNRCV LNWFGDWSTE
3110 3120 3130 3140 3150
ALYQVGKEFT SKMDLEKPNY IVPDYMPVVY DKLPQPPSHR EAIVNSCVFV
3160 3170 3180 3190 3200
HQTLHQANAR LAKRGGRTMA ITPRHYLDFI NHYANLFHEK RSELEEQQMH
3210 3220 3230 3240 3250
LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL KKMVKDQQEA
3260 3270 3280 3290 3300
EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAVI EAQNAVKSIK
3310 3320 3330 3340 3350
KQHLVEVRSM ANPPAAVKLA LESICLLLGE STTDWKQIRS IIMRENFIPT
3360 3370 3380 3390 3400
IVNFSAEEIS DAIREKMKKN YMSNPSYNYE IVNRASLACG PMVKWAIAQL
3410 3420 3430 3440 3450
NYADMLKRVE PLRNELQKLE DDAKDNQQKA NEVEQMIRDL EASIARYKEE
3460 3470 3480 3490 3500
YAVLISEAQA IKADLAAVEA KVNRSTALLK SLSAERERWE KTSETFKNQM
3510 3520 3530 3540 3550
STIAGDCLLS AAFIAYAGYF DQQMRQNLFT TWSHHLQQAN IQFRTDIART
3560 3570 3580 3590 3600
EYLSNADERL RWQASSLPAD DLCTENAIML KRFNRYPLII DPSGQATEFI
3610 3620 3630 3640 3650
MNEYKDRKIT RTSFLDDAFR KNLESALRFG NPLLVQDVES YDPVLNPVLN
3660 3670 3680 3690 3700
REVRRTGGRV LITLGDQDID LSPSFVIFLS TRDPTVEFPP DLCSRVTFVN
3710 3720 3730 3740 3750
FTVTRSSLQS QCLNEVLKAE RPDVDEKRSD LLKLQGEFQL RLRQLEKSLL
3760 3770 3780 3790 3800
QALNEVKGRI LDDDTIITTL ENLKREAAEV TRKVEETDIV MQEVETVSQQ
3810 3820 3830 3840 3850
YLPLSTACSS IYFTMESLKQ IHFLYQYSLQ FFLDIYHNVL YENPNLKGVT
3860 3870 3880 3890 3900
DHTQRLSIIT KDLFQVAFNR VARGMLHQDH ITFAMLLARI KLKGTVGEPT
3910 3920 3930 3940 3950
YDAEFQHFLR GNEIVLSAGS TPRIQGLTVE QAEAVVRLSC LPAFKDLIAK
3960 3970 3980 3990 4000
VQADEQFGIW LDSSSPEQTV PYLWSEETPA TPIGQAIHRL LLIQAFRPDR
4010 4020 4030 4040 4050
LLAMAHMFVS TNLGESFMSI MEQPLDLTHI VGTEVKPNTP VLMCSVPGYD
4060 4070 4080 4090 4100
ASGHVEDLAA EQNTQITSIA IGSAEGFNQA DKAINTAVKS GRWVMLKNVH
4110 4120 4130 4140 4150
LAPGWLMQLE KKLHSLQPHA CFRLFLTMEI NPKVPVNLLR AGRIFVFEPP
4160 4170 4180 4190 4200
PGVKANMLRT FSSIPVSRIC KSPNERARLY FLLAWFHAII QERLRYAPLG
4210 4220 4230 4240 4250
WSKKYEFGES DLRSACDTVD TWLDDTAKGR QNISPDKIPW SALKTLMAQS
4260 4270 4280 4290 4300
IYGGRVDNEF DQRLLNTFLE RLFTTRSFDS EFKLACKVDG HKDIQMPDGI
4310 4320 4330 4340 4350
RREEFVQWVE LLPDTQTPSW LGLPNNAERV LLTTQGVDMI SKMLKMQMLE
4360 4370 4380 4390 4400
DEDDLAYAET EKKTRTDSTS DGRPAWMRTL HTTASNWLHL IPQTLSHLKR
4410 4420 4430 4440 4450
TVENIKDPLF RFFEREVKMG AKLLQDVRQD LADVVQVCEG KKKQTNYLRT
4460 4470 4480 4490 4500
LINELVKGIL PRSWSHYTVP AGMTVIQWVS DFSERIKQLQ NISLAAASGG
4510 4520 4530 4540 4550
AKELKNIHVC LGGLFVPEAY ITATRQYVAQ ANSWSLEELC LEVNVTTSQG
4560 4570 4580 4590 4600
ATLDACSFGV TGLKLQGATC NNNKLSLSNA ISTALPLTQL RWVKQTNTEK
4610 4620 4630 4640
KASVVTLPVY LNFTRADLIF TVDFEIATKE DPRSFYERGV AVLCTE
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. 1 Publication
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 2215-2243, 2587-2622, 3266-3429, 3471-3840, 4038-4330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108117. 109 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 non-syndromic intellectual disability.
PharmGKBi PA27432.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5245.
GeneTreei ENSGT00760000118964.
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

Bgeei Q14204.
CleanExi HS_DYNC1H1.
ExpressionAtlasi Q14204. baseline and differential.
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: October 29, 2014
This is version 148 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