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Q14204 (DYHC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic dynein 1 heavy chain 1
Alternative name(s):
Cytoplasmic dynein heavy chain 1
Dynein heavy chain, cytosolic
Gene names
Name:DYNC1H1
Synonyms:DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4646 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cytoplasmcytoskeleton.

Domain

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.

Involvement in disease

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. Ref.16

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. Ref.15 Ref.17 Ref.20 Ref.21

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. Ref.18 Ref.19

Sequence similarities

Belongs to the dynein heavy chain family.

Sequence caution

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

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Cytoskeleton
Dynein
Microtubule
   Coding sequence diversityPolymorphism
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Mental retardation
Neurodegeneration
Neuropathy
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic mRNA processing body assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

microtubule-based movement

Inferred from electronic annotation. Source: InterPro

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic spindle organization

Non-traceable author statement Ref.6. Source: UniProtKB

stress granule assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytoplasmic dynein complex

Non-traceable author statement Ref.5. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from electronic annotation. Source: InterPro

microtubule motor activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 46464645Cytoplasmic dynein 1 heavy chain 1
PRO_0000114627

Regions

Nucleotide binding1906 – 19138ATP Potential
Nucleotide binding2224 – 22318ATP Potential
Nucleotide binding2595 – 26028ATP Potential
Nucleotide binding2937 – 29448ATP Potential
Region53 – 18671815Stem By similarity
Region448 – 703256Interaction with DYNC1I2 By similarity
Region651 – 802152Interaction with DYNC1LI2 By similarity
Region1868 – 2099232AAA 1 By similarity
Region2180 – 2452273AAA 2 By similarity
Region2556 – 2805250AAA 3 By similarity
Region2899 – 3168270AAA 4 By similarity
Region3189 – 3500312Stalk By similarity
Region3553 – 3782230AAA 5 By similarity
Region4005 – 4221217AAA 6 By similarity
Coiled coil181 – 20222 Potential
Coiled coil455 – 47824 Potential
Coiled coil543 – 56624 Potential
Coiled coil1171 – 125282 Potential
Coiled coil1357 – 137317 Potential
Coiled coil3189 – 327587 Potential
Coiled coil3396 – 3500105 Potential
Coiled coil3737 – 380064 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.14
Modified residue11251N6-acetyllysine Ref.11
Modified residue34801N6-acetyllysine Ref.11
Modified residue42831N6-acetyllysine Ref.11
Modified residue43681Phosphoserine Ref.9

Natural variations

Natural variant1291K → I in MRD13. Ref.21
VAR_070580
Natural variant1421E → A. Ref.20
VAR_069437
Natural variant3061H → R in CMT2O and SMALED1. Ref.16 Ref.18
VAR_066651
Natural variant5841I → L in SMALED1; disrupts dynein complex stability and function. Ref.19
VAR_067820
Natural variant659 – 6624Missing in MRD13.
VAR_070581
Natural variant6711K → E in SMALED1. Ref.19
VAR_067821
Natural variant9701Y → C in SMALED1. Ref.19
VAR_067822
Natural variant12501V → L. Ref.20
VAR_069438
Natural variant15181E → K in MRD13. Ref.17 Ref.20
VAR_067823
Natural variant15671R → Q in MRD13. Ref.21
VAR_070582
Natural variant19621R → C in MRD13. Ref.21
VAR_070583
Natural variant22471V → M. Ref.20
VAR_069439
Natural variant32411K → T in MRD13. Ref.21
VAR_070584
Natural variant33361K → N in MRD13; shows a substantial reduction in the microtubule binding affinity compared to the wild-type control protein. Ref.21
VAR_070585
Natural variant33441R → Q in MRD13. Ref.21
VAR_070586
Natural variant33841R → Q in MRD13; shows a substantial reduction in the microtubule binding affinity compared to the wild-type control protein. Ref.21
VAR_070587
Natural variant38221H → P in MRD13; de novo mutation. Ref.15
VAR_065085
Natural variant39021D → N. Ref.4
Corresponds to variant rs17512818 [ dbSNP | Ensembl ].
VAR_020889
Natural variant40291H → Q. Ref.1 Ref.4
Corresponds to variant rs10129889 [ dbSNP | Ensembl ].
VAR_020890
Natural variant41431R → C. Ref.20
VAR_069440
Natural variant42851A → S. Ref.20
VAR_069441
Natural variant44211A → T. Ref.20
VAR_069442
Natural variant45071I → S. Ref.20
VAR_069443
Natural variant46031S → G. Ref.20
VAR_069444

Experimental info

Sequence conflict1778 – 17792LH → SD in AAB09727. Ref.5
Sequence conflict19411M → R in AAB09727. Ref.5
Sequence conflict20251R → N in AAB09727. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q14204 [UniParc].

Last modified January 4, 2005. Version 5.
Checksum: D4D4E15DFBDE4797

FASTA4,646532,408
        10         20         30         40         50         60 
MSEPGGGGGE DGSAGLEVSA VQNVADVSVL QKHLRKLVPL LLEDGGEAPA ALEAALEEKS 

        70         80         90        100        110        120 
ALEQMRKFLS DPQVHTVLVE RSTLKEDVGD EGEEEKEFIS YNINIDIHYG VKSNSLAFIK 

       130        140        150        160        170        180 
RTPVIDADKP VSSQLRVLTL SEDSPYETLH SFISNAVAPF FKSYIRESGK ADRDGDKMAP 

       190        200        210        220        230        240 
SVEKKIAELE MGLLHLQQNI EIPEISLPIH PMITNVAKQC YERGEKPKVT DFGDKVEDPT 

       250        260        270        280        290        300 
FLNQLQSGVN RWIREIQKVT KLDRDPASGT ALQEISFWLN LERALYRIQE KRESPEVLLT 

       310        320        330        340        350        360 
LDILKHGKRF HATVSFDTDT GLKQALETVN DYNPLMKDFP LNDLLSATEL DKIRQALVAI 

       370        380        390        400        410        420 
FTHLRKIRNT KYPIQRALRL VEAISRDLSS QLLKVLGTRK LMHVAYEEFE KVMVACFEVF 

       430        440        450        460        470        480 
QTWDDEYEKL QVLLRDIVKR KREENLKMVW RINPAHRKLQ ARLDQMRKFR RQHEQLRAVI 

       490        500        510        520        530        540 
VRVLRPQVTA VAQQNQGEVP EPQDMKVAEV LFDAADANAI EEVNLAYENV KEVDGLDVSK 

       550        560        570        580        590        600 
EGTEAWEAAM KRYDERIDRV ETRITARLRD QLGTAKNANE MFRIFSRFNA LFVRPHIRGA 

       610        620        630        640        650        660 
IREYQTQLIQ RVKDDIESLH DKFKVQYPQS QACKMSHVRD LPPVSGSIIW AKQIDRQLTA 

       670        680        690        700        710        720 
YMKRVEDVLG KGWENHVEGQ KLKQDGDSFR MKLNTQEIFD DWARKVQQRN LGVSGRIFTI 

       730        740        750        760        770        780 
ESTRVRGRTG NVLKLKVNFL PEIITLSKEV RNLKWLGFRV PLAIVNKAHQ ANQLYPFAIS 

       790        800        810        820        830        840 
LIESVRTYER TCEKVEERNT ISLLVAGLKK EVQALIAEGI ALVWESYKLD PYVQRLAETV 

       850        860        870        880        890        900 
FNFQEKVDDL LIIEEKIDLE VRSLETCMYD HKTFSEILNR VQKAVDDLNL HSYSNLPIWV 

       910        920        930        940        950        960 
NKLDMEIERI LGVRLQAGLR AWTQVLLGQA EDKAEVDMDT DAPQVSHKPG GEPKIKNVVH 

       970        980        990       1000       1010       1020 
ELRITNQVIY LNPPIEECRY KLYQEMFAWK MVVLSLPRIQ SQRYQVGVHY ELTEEEKFYR 

      1030       1040       1050       1060       1070       1080 
NALTRMPDGP VALEESYSAV MGIVSEVEQY VKVWLQYQCL WDMQAENIYN RLGEDLNKWQ 

      1090       1100       1110       1120       1130       1140 
ALLVQIRKAR GTFDNAETKK EFGPVVIDYG KVQSKVNLKY DSWHKEVLSK FGQMLGSNMT 

      1150       1160       1170       1180       1190       1200 
EFHSQISKSR QELEQHSVDT ASTSDAVTFI TYVQSLKRKI KQFEKQVELY RNGQRLLEKQ 

      1210       1220       1230       1240       1250       1260 
RFQFPPSWLY IDNIEGEWGA FNDIMRRKDS AIQQQVANLQ MKIVQEDRAV ESRTTDLLTD 

      1270       1280       1290       1300       1310       1320 
WEKTKPVTGN LRPEEALQAL TIYEGKFGRL KDDREKCAKA KEALELTDTG LLSGSEERVQ 

      1330       1340       1350       1360       1370       1380 
VALEELQDLK GVWSELSKVW EQIDQMKEQP WVSVQPRKLR QNLDALLNQL KSFPARLRQY 

      1390       1400       1410       1420       1430       1440 
ASYEFVQRLL KGYMKINMLV IELKSEALKD RHWKQLMKRL HVNWVVSELT LGQIWDVDLQ 

      1450       1460       1470       1480       1490       1500 
KNEAIVKDVL LVAQGEMALE EFLKQIREVW NTYELDLVNY QNKCRLIRGW DDLFNKVKEH 

      1510       1520       1530       1540       1550       1560 
INSVSAMKLS PYYKVFEEDA LSWEDKLNRI MALFDVWIDV QRRWVYLEGI FTGSADIKHL 

      1570       1580       1590       1600       1610       1620 
LPVETQRFQS ISTEFLALMK KVSKSPLVMD VLNIQGVQRS LERLADLLGK IQKALGEYLE 

      1630       1640       1650       1660       1670       1680 
RERSSFPRFY FVGDEDLLEI IGNSKNVAKL QKHFKKMFAG VSSIILNEDN SVVLGISSRE 

      1690       1700       1710       1720       1730       1740 
GEEVMFKTPV SITEHPKINE WLTLVEKEMR VTLAKLLAES VTEVEIFGKA TSIDPNTYIT 

      1750       1760       1770       1780       1790       1800 
WIDKYQAQLV VLSAQIAWSE NVETALSSMG GGGDAAPLHS VLSNVEVTLN VLADSVLMEQ 

      1810       1820       1830       1840       1850       1860 
PPLRRRKLEH LITELVHQRD VTRSLIKSKI DNAKSFEWLS QMRFYFDPKQ TDVLQQLSIQ 

      1870       1880       1890       1900       1910       1920 
MANAKFNYGF EYLGVQDKLV QTPLTDRCYL TMTQALEARL GGSPFGPAGT GKTESVKALG 

      1930       1940       1950       1960       1970       1980 
HQLGRFVLVF NCDETFDFQA MGRIFVGLCQ VGAWGCFDEF NRLEERMLSA VSQQVQCIQE 

      1990       2000       2010       2020       2030       2040 
ALREHSNPNY DKTSAPITCE LLNKQVKVSP DMAIFITMNP GYAGRSNLPD NLKKLFRSLA 

      2050       2060       2070       2080       2090       2100 
MTKPDRQLIA QVMLYSQGFR TAEVLANKIV PFFKLCDEQL SSQSHYDFGL RALKSVLVSA 

      2110       2120       2130       2140       2150       2160 
GNVKRERIQK IKREKEERGE AVDEGEIAEN LPEQEILIQS VCETMVPKLV AEDIPLLFSL 

      2170       2180       2190       2200       2210       2220 
LSDVFPGVQY HRGEMTALRE ELKKVCQEMY LTYGDGEEVG GMWVEKVLQL YQITQINHGL 

      2230       2240       2250       2260       2270       2280 
MMVGPSGSGK SMAWRVLLKA LERLEGVEGV AHIIDPKAIS KDHLYGTLDP NTREWTDGLF 

      2290       2300       2310       2320       2330       2340 
THVLRKIIDS VRGELQKRQW IVFDGDVDPE WVENLNSVLD DNKLLTLPNG ERLSLPPNVR 

      2350       2360       2370       2380       2390       2400 
IMFEVQDLKY ATLATVSRCG MVWFSEDVLS TDMIFNNFLA RLRSIPLDEG EDEAQRRRKG 

      2410       2420       2430       2440       2450       2460 
KEDEGEEAAS PMLQIQRDAA TIMQPYFTSN GLVTKALEHA FQLEHIMDLT RLRCLGSLFS 

      2470       2480       2490       2500       2510       2520 
MLHQACRNVA QYNANHPDFP MQIEQLERYI QRYLVYAILW SLSGDSRLKM RAELGEYIRR 

      2530       2540       2550       2560       2570       2580 
ITTVPLPTAP NIPIIDYEVS ISGEWSPWQA KVPQIEVETH KVAAPDVVVP TLDTVRHEAL 

      2590       2600       2610       2620       2630       2640 
LYTWLAEHKP LVLCGPPGSG KTMTLFSALR ALPDMEVVGL NFSSATTPEL LLKTFDHYCE 

      2650       2660       2670       2680       2690       2700 
YRRTPNGVVL APVQLGKWLV LFCDEINLPD MDKYGTQRVI SFIRQMVEHG GFYRTSDQTW 

      2710       2720       2730       2740       2750       2760 
VKLERIQFVG ACNPPTDPGR KPLSHRFLRH VPVVYVDYPG PASLTQIYGT FNRAMLRLIP 

      2770       2780       2790       2800       2810       2820 
SLRTYAEPLT AAMVEFYTMS QERFTQDTQP HYIYSPREMT RWVRGIFEAL RPLETLPVEG 

      2830       2840       2850       2860       2870       2880 
LIRIWAHEAL RLFQDRLVED EERRWTDENI DTVALKHFPN IDREKAMSRP ILYSNWLSKD 

      2890       2900       2910       2920       2930       2940 
YIPVDQEELR DYVKARLKVF YEEELDVPLV LFNEVLDHVL RIDRIFRQPQ GHLLLIGVSG 

      2950       2960       2970       2980       2990       3000 
AGKTTLSRFV AWMNGLSVYQ IKVHRKYTGE DFDEDLRTVL RRSGCKNEKI AFIMDESNVL 

      3010       3020       3030       3040       3050       3060 
DSGFLERMNT LLANGEVPGL FEGDEYATLM TQCKEGAQKE GLMLDSHEEL YKWFTSQVIR 

      3070       3080       3090       3100       3110       3120 
NLHVVFTMNP SSEGLKDRAA TSPALFNRCV LNWFGDWSTE ALYQVGKEFT SKMDLEKPNY 

      3130       3140       3150       3160       3170       3180 
IVPDYMPVVY DKLPQPPSHR EAIVNSCVFV HQTLHQANAR LAKRGGRTMA ITPRHYLDFI 

      3190       3200       3210       3220       3230       3240 
NHYANLFHEK RSELEEQQMH LNVGLRKIKE TVDQVEELRR DLRIKSQELE VKNAAANDKL 

      3250       3260       3270       3280       3290       3300 
KKMVKDQQEA EKKKVMSQEI QEQLHKQQEV IADKQMSVKE DLDKVEPAVI EAQNAVKSIK 

      3310       3320       3330       3340       3350       3360 
KQHLVEVRSM ANPPAAVKLA LESICLLLGE STTDWKQIRS IIMRENFIPT IVNFSAEEIS 

      3370       3380       3390       3400       3410       3420 
DAIREKMKKN YMSNPSYNYE IVNRASLACG PMVKWAIAQL NYADMLKRVE PLRNELQKLE 

      3430       3440       3450       3460       3470       3480 
DDAKDNQQKA NEVEQMIRDL EASIARYKEE YAVLISEAQA IKADLAAVEA KVNRSTALLK 

      3490       3500       3510       3520       3530       3540 
SLSAERERWE KTSETFKNQM STIAGDCLLS AAFIAYAGYF DQQMRQNLFT TWSHHLQQAN 

      3550       3560       3570       3580       3590       3600 
IQFRTDIART EYLSNADERL RWQASSLPAD DLCTENAIML KRFNRYPLII DPSGQATEFI 

      3610       3620       3630       3640       3650       3660 
MNEYKDRKIT RTSFLDDAFR KNLESALRFG NPLLVQDVES YDPVLNPVLN REVRRTGGRV 

      3670       3680       3690       3700       3710       3720 
LITLGDQDID LSPSFVIFLS TRDPTVEFPP DLCSRVTFVN FTVTRSSLQS QCLNEVLKAE 

      3730       3740       3750       3760       3770       3780 
RPDVDEKRSD LLKLQGEFQL RLRQLEKSLL QALNEVKGRI LDDDTIITTL ENLKREAAEV 

      3790       3800       3810       3820       3830       3840 
TRKVEETDIV MQEVETVSQQ YLPLSTACSS IYFTMESLKQ IHFLYQYSLQ FFLDIYHNVL 

      3850       3860       3870       3880       3890       3900 
YENPNLKGVT DHTQRLSIIT KDLFQVAFNR VARGMLHQDH ITFAMLLARI KLKGTVGEPT 

      3910       3920       3930       3940       3950       3960 
YDAEFQHFLR GNEIVLSAGS TPRIQGLTVE QAEAVVRLSC LPAFKDLIAK VQADEQFGIW 

      3970       3980       3990       4000       4010       4020 
LDSSSPEQTV PYLWSEETPA TPIGQAIHRL LLIQAFRPDR LLAMAHMFVS TNLGESFMSI 

      4030       4040       4050       4060       4070       4080 
MEQPLDLTHI VGTEVKPNTP VLMCSVPGYD ASGHVEDLAA EQNTQITSIA IGSAEGFNQA 

      4090       4100       4110       4120       4130       4140 
DKAINTAVKS GRWVMLKNVH LAPGWLMQLE KKLHSLQPHA CFRLFLTMEI NPKVPVNLLR 

      4150       4160       4170       4180       4190       4200 
AGRIFVFEPP PGVKANMLRT FSSIPVSRIC KSPNERARLY FLLAWFHAII QERLRYAPLG 

      4210       4220       4230       4240       4250       4260 
WSKKYEFGES DLRSACDTVD TWLDDTAKGR QNISPDKIPW SALKTLMAQS IYGGRVDNEF 

      4270       4280       4290       4300       4310       4320 
DQRLLNTFLE RLFTTRSFDS EFKLACKVDG HKDIQMPDGI RREEFVQWVE LLPDTQTPSW 

      4330       4340       4350       4360       4370       4380 
LGLPNNAERV LLTTQGVDMI SKMLKMQMLE DEDDLAYAET EKKTRTDSTS DGRPAWMRTL 

      4390       4400       4410       4420       4430       4440 
HTTASNWLHL IPQTLSHLKR TVENIKDPLF RFFEREVKMG AKLLQDVRQD LADVVQVCEG 

      4450       4460       4470       4480       4490       4500 
KKKQTNYLRT LINELVKGIL PRSWSHYTVP AGMTVIQWVS DFSERIKQLQ NISLAAASGG 

      4510       4520       4530       4540       4550       4560 
AKELKNIHVC LGGLFVPEAY ITATRQYVAQ ANSWSLEELC LEVNVTTSQG ATLDACSFGV 

      4570       4580       4590       4600       4610       4620 
TGLKLQGATC NNNKLSLSNA ISTALPLTQL RWVKQTNTEK KASVVTLPVY LNFTRADLIF 

      4630       4640 
TVDFEIATKE DPRSFYERGV AVLCTE 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"A de novo paradigm for mental retardation."
Vissers L.E., de Ligt J., Gilissen C., Janssen I., Steehouwer M., de Vries P., van Lier B., Arts P., Wieskamp N., del Rosario M., van Bon B.W., Hoischen A., de Vries B.B., Brunner H.G., Veltman J.A.
Nat. Genet. 42:1109-1112(2010) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in DYNC1H1 cause severe intellectual disability with neuronal migration defects."
Willemsen M.H., Vissers L.E., Willemsen M.A., van Bon B.W., Kroes T., de Ligt J., de Vries B.B., Schoots J., Lugtenberg D., Hamel B.C., van Bokhoven H., Brunner H.G., Veltman J.A., Kleefstra T.
J. Med. Genet. 49:179-183(2012) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in the tail domain of DYNC1H1 cause dominant spinal muscular atrophy."
Harms M.B., Ori-McKenney K.M., Scoto M., Tuck E.P., Bell S., Ma D., Masi S., Allred P., Al-Lozi M., Reilly M.M., Miller L.J., Jani-Acsadi A., Pestronk A., Shy M.E., Muntoni F., Vallee R.B., Baloh R.H.
Neurology 78:1714-1720(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SMALED1 LEU-584; GLU-671 AND CYS-970, CHARACTERIZATION OF VARIANT SMALED1 LEU-584.
[20]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
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]"Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of cortical development and microcephaly."
Poirier K., Lebrun N., Broix L., Tian G., Saillour Y., Boscheron C., Parrini E., Valence S., Pierre B.S., Oger M., Lacombe D., Genevieve D., Fontana E., Darra F., Cances C., Barth M., Bonneau D., Bernadina B.D. expand/collapse author list , N'guyen S., Gitiaux C., Parent P., des Portes V., Pedespan J.M., Legrez V., Castelnau-Ptakine L., Nitschke P., Hieu T., Masson C., Zelenika D., Andrieux A., Francis F., Guerrini R., Cowan N.J., Bahi-Buisson N., Chelly J.
Nat. Genet. 45:639-647(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA49019.
G02529.
RefSeqNP_001367.2. NM_001376.4.
UniGeneHs.614080.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BORmodel-A3200-3299[»]
B3398-3497[»]
2BOTmodel-A3197-3296[»]
B3398-3497[»]
ProteinModelPortalQ14204.
SMRQ14204. Positions 1905-1965, 2215-2240, 2337-2365, 2591-2627, 2928-2998, 3229-3437, 4038-4330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108117. 102 interactions.
IntActQ14204. 33 interactions.
MINTMINT-5003694.
STRING9606.ENSP00000348965.

PTM databases

PhosphoSiteQ14204.

Polymorphism databases

DMDM57015308.

Proteomic databases

PaxDbQ14204.
PRIDEQ14204.

Protocols and materials databases

DNASU1778.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360184; ENSP00000348965; ENSG00000197102.
GeneID1778.
KEGGhsa:1778.
UCSCuc001yks.2. human.

Organism-specific databases

CTD1778.
GeneCardsGC14P102430.
HGNCHGNC:2961. DYNC1H1.
HPACAB010443.
HPA003742.
MIM158600. phenotype.
600112. gene.
614228. phenotype.
614563. phenotype.
neXtProtNX_Q14204.
Orphanet284232. Autosomal dominant Charcot-Marie-Tooth disease type 2O.
209341. Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures.
178469. Autosomal dominant nonsyndromic intellectual deficit.
PharmGKBPA27432.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5245.
HOGENOMHOG000176055.
HOVERGENHBG096595.
InParanoidQ14204.
KOK10413.
OMAICQGEKK.
OrthoDBEOG76471R.
PhylomeDBQ14204.
TreeFamTF101165.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ14204.
BgeeQ14204.
CleanExHS_DYNC1H1.
GenevestigatorQ14204.

Family and domain databases

Gene3D3.40.50.300. 5 hits.
InterProIPR003593. 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]
PANTHERPTHR10676. PTHR10676. 1 hit.
PfamPF07728. 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]
SMARTSM00382. AAA. 4 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 5 hits.
ProtoNetSearch...

Other

ChiTaRSDYNC1H1. human.
GeneWikiDYNC1H1.
GenomeRNAi1778.
NextBio7239.
PROQ14204.
SOURCESearch...

Entry information

Entry nameDYHC1_HUMAN
AccessionPrimary (citable) accession number: Q14204
Secondary accession number(s): B0I1R0 expand/collapse secondary AC list , Q6DKQ7, Q8WU28, Q92814, Q9Y4G5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 142 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM