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P38650

- DYHC1_RAT

UniProt

P38650 - DYHC1_RAT

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Protein

Cytoplasmic dynein 1 heavy chain 1

Gene

Dync1h1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1904 – 19118ATPSequence Analysis
Nucleotide bindingi2222 – 22298ATPSequence Analysis
Nucleotide bindingi2593 – 26008ATPSequence Analysis
Nucleotide bindingi2935 – 29428ATPSequence Analysis

GO - Molecular functioni

  1. ATPase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. microtubule motor activity Source: InterPro

GO - Biological processi

  1. microtubule-based movement Source: InterPro
  2. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic dynein 1 heavy chain 1
Alternative name(s):
Cytoplasmic dynein heavy chain 1
Dynein heavy chain, cytosolic
MAP 1C
Gene namesi
Name:Dync1h1
Synonyms:Dhc1, Dnch1, Dnchc1, Dnec1, Dyhc, Map1c
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2511. Dync1h1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. dynein complex Source: UniProtKB-KW
  3. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 46444643Cytoplasmic dynein 1 heavy chain 1PRO_0000114629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei1123 – 11231N6-acetyllysineBy similarity
Modified residuei3478 – 34781N6-acetyllysineBy similarity
Modified residuei4281 – 42811N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP38650.
PRIDEiP38650.

Expressioni

Gene expression databases

GenevestigatoriP38650.

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 DYNC1I2.2 Publications

Protein-protein interaction databases

BioGridi248131. 6 interactions.
IntActiP38650. 4 interactions.
MINTiMINT-4564742.

Structurei

3D structure databases

ProteinModelPortaliP38650.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 18651864StemBy similarityAdd
BLAST
Regioni446 – 701256Interaction with DYNC1I2Add
BLAST
Regioni649 – 800152Interaction with DYNC1LI2Add
BLAST
Regioni1866 – 2097232AAA 1By similarityAdd
BLAST
Regioni2178 – 2450273AAA 2By similarityAdd
BLAST
Regioni2554 – 2803250AAA 3By similarityAdd
BLAST
Regioni2897 – 3166270AAA 4By similarityAdd
BLAST
Regioni3187 – 3498312StalkBy similarityAdd
BLAST
Regioni3551 – 3780230AAA 5By similarityAdd
BLAST
Regioni4003 – 4219217AAA 6By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili48 – 6922Sequence AnalysisAdd
BLAST
Coiled coili179 – 20022Sequence AnalysisAdd
BLAST
Coiled coili453 – 47624Sequence AnalysisAdd
BLAST
Coiled coili541 – 56424Sequence AnalysisAdd
BLAST
Coiled coili1169 – 120133Sequence AnalysisAdd
BLAST
Coiled coili1229 – 125022Sequence AnalysisAdd
BLAST
Coiled coili1355 – 137117Sequence AnalysisAdd
BLAST
Coiled coili3187 – 327387Sequence AnalysisAdd
BLAST
Coiled coili3394 – 3498105Sequence AnalysisAdd
BLAST
Coiled coili3735 – 379864Sequence 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.
HOGENOMiHOG000176055.
HOVERGENiHBG096595.
InParanoidiP38650.
KOiK10413.
PhylomeDBiP38650.

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.

P38650-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MSETGGGEDG SAGLEVSAVQ NVADVSVLQK HLRKLVPLLL EDGGDAPAAL
60 70 80 90 100
EAALEEKSAL EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN
110 120 130 140 150
INIDIHYGVK SNSLAFIKRA PVIDADKPVS SQLRVLTLSE DSPYETLHSF
160 170 180 190 200
ISNAVAPFFK SYIRESGKAD RDGDKMAPSV EKKIAELEMG LLHLQQNIEI
210 220 230 240 250
PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL NQLQSGVNRW
260 270 280 290 300
IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD
310 320 330 340 350
ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK
360 370 380 390 400
IRQALVAIFT HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM
410 420 430 440 450
HVAYEEFEKV MVACFEVFQT WDDEYEKLQV LLRDIVKRKR EENLKMVWRI
460 470 480 490 500
NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR VLRPQVTAVA QQNQGEAPEP
510 520 530 540 550
QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG TEAWEAAMKR
560 570 580 590 600
YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR
610 620 630 640 650
EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK
660 670 680 690 700
QIDRQLTAYM KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW
710 720 730 740 750
ARKVQQRNLG VSGRIFTIES ARVRGRSGNV LKLKVNFLPE IITLSKEVRN
760 770 780 790 800
LKWLGFRVPL AIVNKAHQAN QLYPFAISLI ESVRTYERTC EKVEERNTIS
810 820 830 840 850
LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN FQEKVDDLLI
860 870 880 890 900
IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK
910 920 930 940 950
LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE
960 970 980 990 1000
PKIKNVVHEL RITNQVIYLN PPIEECRYKL YQEMFAWKMI VLSLPRIQSQ
1010 1020 1030 1040 1050
RYQVGVHYEL TEEEKFYRNA LTRSRDGPVA LEESYSAVMG IVTEVEQYVK
1060 1070 1080 1090 1100
VWLQYQCLWD MQAENIYNRL GEDLSKWQAL LVQIRRARGT FDNAETKKEF
1110 1120 1130 1140 1150
GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF HSQISKSRQE
1160 1170 1180 1190 1200
LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF
1210 1220 1230 1240 1250
QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES
1260 1270 1280 1290 1300
RTTDLLTDWE KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE
1310 1320 1330 1340 1350
ALELTDTGLL SGSEERVQVA LEELQDLKGV WSELSKVWEQ IDQMKEQPWV
1360 1370 1380 1390 1400
SVQPRKLRQN LDGLLNQLKN FPARLRQYAS YEFVQRLLKG YMKINMLVIE
1410 1420 1430 1440 1450
LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN EAIVKDVLLV
1460 1470 1480 1490 1500
AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN
1510 1520 1530 1540 1550
SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT
1560 1570 1580 1590 1600
GSADIKHLLP VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE
1610 1620 1630 1640 1650
RLADLLGKIQ KALGEYLERE RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK
1660 1670 1680 1690 1700
HFKKMFAGVS SIILNEDSSV VLGISSREGE EVMFKTPVSI TEHPKINEWL
1710 1720 1730 1740 1750
TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI DKYQAQLVVL
1760 1770 1780 1790 1800
SAQIAWSENV ENALSNVGGG GNVGPLQSVL SNVEVTLNVL ADSVLMEQPP
1810 1820 1830 1840 1850
LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD
1860 1870 1880 1890 1900
VLQQLSIQMA NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG
1910 1920 1930 1940 1950
SPFGPAGTGK TESVKALGHQ LGRFVLVFNC DETFDFQAMG RIFVGLCQVG
1960 1970 1980 1990 2000
AWGCFDEFNR LEERMLSAVS QQVQCIQEAL REHSNPNYDK TSAPITCELL
2010 2020 2030 2040 2050
NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT KPDRQLIAQV
2060 2070 2080 2090 2100
MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSPGN
2110 2120 2130 2140 2150
VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSFC ETMVPKLVAE
2160 2170 2180 2190 2200
DIPLLFSLLS DVFPGVQYHR GEMTDLREEL KKVCKEMYLT YGDGEEVGGM
2210 2220 2230 2240 2250
WVEKVLQLYQ ITQINHGLMM VGPSGSGKSM AWRVLLKALE RLEGVEGVAH
2260 2270 2280 2290 2300
IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDNVR GELQKRQWIV
2310 2320 2330 2340 2350
FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM FEVQDLKYAT
2360 2370 2380 2390 2400
LATVSRCGMV WFSEDLLSTD MIFNNFLARL RTIPLDEGED EAQRRRKGKE
2410 2420 2430 2440 2450
DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL
2460 2470 2480 2490 2500
RCLGSLFSML HQGCRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL
2510 2520 2530 2540 2550
SGDSRLKMRA ELGEYIRRIT TVPLPTAPNI PIIDYEVSIS GEWSPWQAKV
2560 2570 2580 2590 2600
PQIEVETHKV AAPDVVVPTL DTVRHEALLY TWLAEHKPLV LCGPPGSGKT
2610 2620 2630 2640 2650
MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR RTPNGVVLAP
2660 2670 2680 2690 2700
VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK
2710 2720 2730 2740 2750
LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN
2760 2770 2780 2790 2800
RAMLRLIPSL RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW
2810 2820 2830 2840 2850
VRGIFEALRP LETLPVEGLI RIWAHEALRL FQDRLVEDEE RRWTDENIDM
2860 2870 2880 2890 2900
VALKHFPNID KEKAMSRPIL YSNWLSKDYI PVDQEELRDY VKARLKVFYE
2910 2920 2930 2940 2950
EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG KTTLSRFVAW
2960 2970 2980 2990 3000
MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS
3010 3020 3030 3040 3050
GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK
3060 3070 3080 3090 3100
WFTSQVIRNL HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL
3110 3120 3130 3140 3150
YQVGKEFTSK MDLEKPNYIV PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ
3160 3170 3180 3190 3200
TLHQANARLA KRGGRTMAIT PRHYLDFINH YANLFHEKRS ELEEQQMHLN
3210 3220 3230 3240 3250
VGLRKIKETV DQVEELRRAL RIKSQELEVK NAAANDKLKK MVKDQQEAEK
3260 3270 3280 3290 3300
KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ
3310 3320 3330 3340 3350
HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV
3360 3370 3380 3390 3400
NFSAEEISDA IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY
3410 3420 3430 3440 3450
ADMLKRVEPL RNELQKLEDD AKDNQQKANE VEQMIRDLEA SIARYKEEYA
3460 3470 3480 3490 3500
VLISEAQAIK ADLAAVEAKV NRSTALLKSL SAERERWEKT SETFKNQMST
3510 3520 3530 3540 3550
IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ FRTDIARTEY
3560 3570 3580 3590 3600
LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN
3610 3620 3630 3640 3650
EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE
3660 3670 3680 3690 3700
VRRTGGRVLI TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT
3710 3720 3730 3740 3750
VTRSSLQSQC LNEVLKAERP DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA
3760 3770 3780 3790 3800
LNEVKGRILD DDTIITTLEN LKREAAEVTR KVEETDIVMQ EVETVSQQYL
3810 3820 3830 3840 3850
PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE NPNLKGATDH
3860 3870 3880 3890 3900
TQRLSVITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTMGEPTYD
3910 3920 3930 3940 3950
AEFQHFLRGK EIVLSAGSTP KVQGLTVEQA EAVARLSCLP AFKDLIAKVQ
3960 3970 3980 3990 4000
ADEQFGIWLE SSSPEQTVPY LWTEETPATP IGQAIHRLLL IQAFRPDRLL
4010 4020 4030 4040 4050
AMAHMFVSTN LGESFMSIME QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS
4060 4070 4080 4090 4100
GHVEDLAAEQ NTQITSIAIG SAEGFNQADK AINTAVKSGR WVMLKNVHLA
4110 4120 4130 4140 4150
PGWLMQLEKK LHSLQPHACF RLFLTMEINP RVPVNLLRAG RIFVFEPPPG
4160 4170 4180 4190 4200
VKANMLRTFS SIPVSRMCKS PNERARLYFL LAWFHAVIQE RLRYAPLGWS
4210 4220 4230 4240 4250
KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY
4260 4270 4280 4290 4300
GGRVDNEFDQ RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR
4310 4320 4330 4340 4350
EEFVQWVELL PDAQTPSWLG LPNNAERVLL TTQGVDMISK MLKMQMLEDE
4360 4370 4380 4390 4400
DDLAYAETEK KTRTDFTSDG RPAWMRTLHT TASNWLHLIP QTLSPLKRTV
4410 4420 4430 4440 4450
ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK KQTNYLRTLI
4460 4470 4480 4490 4500
NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAAAGGAK
4510 4520 4530 4540 4550
ELKNIHVCLG ALFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSTT
4560 4570 4580 4590 4600
LDACSFGVTG LKLQGATCSN NKLSLSNAIS TVLPLTQLRW GKQTSAEKKA
4610 4620 4630 4640
SVVTLPVYLN FTRADLIFTV DFEIATKEDP RSFYERGVAV LCTE
Length:4,644
Mass (Da):532,252
Last modified:February 1, 1995 - v1
Checksum:i8C6ABDBEDF875D82
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1024 – 10252SR → MP in AAA41103. (PubMed:7684232)Curated
Sequence conflicti1772 – 17721N → D in AAA41103. (PubMed:7684232)Curated
Sequence conflicti2098 – 20981P → A in AAA41103. (PubMed:7684232)Curated
Sequence conflicti2139 – 21391F → V in AAA41103. (PubMed:7684232)Curated
Sequence conflicti2175 – 21751D → A in AAA41103. (PubMed:7684232)Curated
Sequence conflicti2185 – 21851K → Q in AAA41103. (PubMed:7684232)Curated
Sequence conflicti2366 – 23661L → V in AAA41103. (PubMed:7684232)Curated
Sequence conflicti2382 – 23821T → S in AAA41103. (PubMed:7684232)Curated
Sequence conflicti2463 – 24631G → A in AAA41103. (PubMed:7684232)Curated
Sequence conflicti3219 – 32191A → D in AAA41103. (PubMed:7684232)Curated
Sequence conflicti4131 – 41311R → K in AAA41103. (PubMed:7684232)Curated
Sequence conflicti4366 – 43661F → S in AAA41103. (PubMed:7684232)Curated
Sequence conflicti4511 – 45111A → G in AAA41103. (PubMed:7684232)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13896 mRNA. Translation: BAA02996.1.
L08505 mRNA. Translation: AAA41103.1.
PIRiA38905.
RefSeqiNP_062099.3. NM_019226.3.
UniGeneiRn.11027.

Genome annotation databases

GeneIDi29489.
KEGGirno:29489.
UCSCiRGD:2511. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13896 mRNA. Translation: BAA02996.1 .
L08505 mRNA. Translation: AAA41103.1 .
PIRi A38905.
RefSeqi NP_062099.3. NM_019226.3.
UniGenei Rn.11027.

3D structure databases

ProteinModelPortali P38650.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248131. 6 interactions.
IntActi P38650. 4 interactions.
MINTi MINT-4564742.

Chemistry

BindingDBi P38650.
ChEMBLi CHEMBL3694.

Proteomic databases

PaxDbi P38650.
PRIDEi P38650.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29489.
KEGGi rno:29489.
UCSCi RGD:2511. rat.

Organism-specific databases

CTDi 1778.
RGDi 2511. Dync1h1.

Phylogenomic databases

eggNOGi COG5245.
HOGENOMi HOG000176055.
HOVERGENi HBG096595.
InParanoidi P38650.
KOi K10413.
PhylomeDBi P38650.

Miscellaneous databases

NextBioi 609363.
PROi P38650.

Gene expression databases

Genevestigatori P38650.

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

  1. "The primary structure of rat brain (cytoplasmic) dynein heavy chain, a cytoplasmic motor enzyme."
    Zhang Z., Tanaka Y., Nonaka S., Aizawa H., Kawasaki H., Nakata T., Hirokawa N.
    Proc. Natl. Acad. Sci. U.S.A. 90:7928-7932(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Brain.
  2. "Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP 1C)."
    Mikami A., Paschal B.M., Mazumdar M., Vallee R.B.
    Neuron 10:787-796(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits."
    Neely M.D., Erickson H.P., Boekelheide K.
    J. Biol. Chem. 265:8691-8698(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  4. "Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding."
    Tynan S.H., Gee M.A., Vallee R.B.
    J. Biol. Chem. 275:32769-32774(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DYNC1LI1; DYNC1LI2 AND DYNC1I2.

Entry informationi

Entry nameiDYHC1_RAT
AccessioniPrimary (citable) accession number: P38650
Secondary accession number(s): Q63178
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3