Q14204 (DYHC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	4646 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton.
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.15 Mental retardation, autosomal dominant 13 (MRD13) [MIM:614563]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative 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.14 Ref.16 Spinal muscular atrophy, lower extremity, autosomal dominant (SMALED) [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. SMALED 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.17 Ref.18
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 process	Transport
Cellular component	Cytoplasm Cytoskeleton Dynein Microtubule
Coding sequence diversity	Polymorphism
Disease	Charcot-Marie-Tooth disease Disease mutation Mental retardation Neurodegeneration Neuropathy
Domain	Coiled coil Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/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 Non-traceable author statement. Source: UniProtKB 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_component	Golgi apparatus Inferred from direct assay. Source: HPA centrosome 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled Non-traceable author statement. Source: UniProtKB microtubule motor activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DISC1	Q9NRI5	3	EBI-356015,EBI-529989
PSEN2	P49810	3	EBI-356015,EBI-2010251

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 4646	4646	Cytoplasmic dynein 1 heavy chain 1		PRO_0000114627
Regions
	Nucleotide binding	1906 – 1913	8	ATP Potential
	Nucleotide binding	2224 – 2231	8	ATP Potential
	Nucleotide binding	2595 – 2602	8	ATP Potential
	Nucleotide binding	2937 – 2944	8	ATP Potential
	Region	53 – 1867	1815	Stem By similarity
	Region	448 – 703	256	Interaction with DYNC1I2 By similarity
	Region	651 – 802	152	Interaction with DYNC1LI2 By similarity
	Region	1868 – 2099	232	AAA 1 By similarity
	Region	2180 – 2452	273	AAA 2 By similarity
	Region	2556 – 2805	250	AAA 3 By similarity
	Region	2899 – 3168	270	AAA 4 By similarity
	Region	3189 – 3500	312	Stalk By similarity
	Region	3553 – 3782	230	AAA 5 By similarity
	Region	4005 – 4221	217	AAA 6 By similarity
	Coiled coil	181 – 202	22	Potential
	Coiled coil	455 – 478	24	Potential
	Coiled coil	543 – 566	24	Potential
	Coiled coil	1171 – 1252	82	Potential
	Coiled coil	1357 – 1373	17	Potential
	Coiled coil	3189 – 3275	87	Potential
	Coiled coil	3396 – 3500	105	Potential
	Coiled coil	3737 – 3800	64	Potential
Amino acid modifications
	Modified residue	1125	1	N6-acetyllysine Ref.11
	Modified residue	3379	1	Phosphotyrosine By similarity
	Modified residue	3480	1	N6-acetyllysine Ref.11
	Modified residue	4218	1	Phosphothreonine By similarity
	Modified residue	4221	1	Phosphothreonine By similarity
	Modified residue	4283	1	N6-acetyllysine Ref.11
	Modified residue	4368	1	Phosphoserine Ref.9
Natural variations
	Natural variant	306	1	H → R in CMT2O and SMALED. Ref.15 Ref.17		VAR_066651
	Natural variant	584	1	I → L in SMALED; disrupts dynein complex stability and function. Ref.18		VAR_067820
	Natural variant	671	1	K → E in SMALED. Ref.18		VAR_067821
	Natural variant	970	1	Y → C in SMALED. Ref.18		VAR_067822
	Natural variant	1518	1	E → K in MRD13. Ref.16		VAR_067823
	Natural variant	3822	1	H → P in MRD13; de novo mutation. Ref.14		VAR_065085
	Natural variant	3902	1	D → N. Ref.4 Corresponds to variant rs17512818 [ dbSNP | Ensembl ].		VAR_020889
	Natural variant	4029	1	H → Q. Ref.1 Ref.4 Corresponds to variant rs10129889 [ dbSNP | Ensembl ].		VAR_020890
Experimental info
	Sequence conflict	1778 – 1779	2	LH → SD in AAB09727. Ref.5
	Sequence conflict	1941	1	M → R in AAB09727. Ref.5
	Sequence conflict	2025	1	R → N in AAB09727. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q14204 [UniParc]. Last modified January 4, 2005. Version 5. Checksum: D4D4E15DFBDE4797	FASTA	4,646	532,408
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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]	"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.
[15]	"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.
[16]	"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.
[17]	"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 SMALED ARG-306.
[18]	"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 SMALED LEU-584; GLU-671 AND CYS-970, CHARACTERIZATION OF VARIANT SMALED LEU-584.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00456969.

PIR

A49019.
G02529.

RefSeq

NP_001367.2. NM_001376.4.

UniGene

Hs.614080.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BOR	model	-	A	3200-3299	[»]
			B	3398-3497	[»]
2BOT	model	-	A	3197-3296	[»]
			B	3398-3497	[»]

ProteinModelPortal

Q14204.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14204. 27 interactions.

MINT

MINT-5003694.

STRING

9606.ENSP00000348965.

PTM databases

PhosphoSite

Q14204.

Polymorphism databases

DMDM

57015308.

Proteomic databases

PaxDb

Q14204.

PRIDE

Q14204.

Protocols and materials databases

DNASU

1778.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000360184; ENSP00000348965; ENSG00000197102.

GeneID

1778.

KEGG

hsa:1778.

UCSC

uc001yks.2. human.

Organism-specific databases

CTD

1778.

GeneCards

GC14P102430.

HGNC

HGNC:2961. DYNC1H1.

HPA

CAB010443.
HPA003742.

MIM

158600. phenotype.
600112. gene.
614228. phenotype.
614563. phenotype.

neXtProt

NX_Q14204.

Orphanet

284232. Autosomal dominant Charcot-Marie-Tooth disease type 2O.
178469. Autosomal dominant nonsyndromic intellectual deficit.
209341. Childhood-onset proximal spinal muscular atrophy, autosomal dominant.

PharmGKB

PA27432.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5245.

HOGENOM

HOG000176055.

HOVERGEN

HBG096595.

InParanoid

Q14204.

KO

K10413.

OMA

ICQGEKK.

OrthoDB

EOG4P5K86.

Enzyme and pathway databases

Pathway_Interaction_DB

lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.

Reactome

REACT_115566. Cell Cycle.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q14204.

Bgee

Q14204.

CleanEx

HS_DYNC1H1.

Genevestigator

Q14204.

GermOnline

ENSG00000197102. Homo sapiens.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR011704. ATPase_dyneun-rel_AAA.
IPR026983. DHC_fam.
IPR025290. DUF4151.
IPR024743. Dynein_HC_stalk.
IPR024317. Dynein_heavy_chain_D4_dom.
IPR004273. Dynein_heavy_dom.
IPR013594. Dynein_heavy_dom-1.
IPR013602. Dynein_heavy_dom-2.
[Graphical view]

PANTHER

PTHR10676. PTHR10676. 1 hit.

Pfam

PF07728. AAA_5. 1 hit.
PF12780. AAA_8. 1 hit.
PF08385. DHC_N1. 1 hit.
PF08393. DHC_N2. 1 hit.
PF13666. DUF4151. 1 hit.
PF03028. Dynein_heavy. 1 hit.
PF12777. MT. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DYNC1H1. human.

GenomeRNAi

1778.

NextBio

7239.

SOURCE

Search...

Entry information

Entry name

DYHC1_HUMAN

Accession

Primary (citable) accession number: Q14204
Secondary accession number(s): B0I1R0 , Q6DKQ7, Q8WU28, Q92814, Q9Y4G5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 132 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.