SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P38650

- DYHC1_RAT

UniProt

P38650 - DYHC1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Cytoplasmic dynein 1 heavy chain 1
Gene
Dync1h1, Dhc1, Dnch1, Dnchc1, Dnec1, Dyhc, Map1c
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 – 19118ATP Reviewed prediction
Nucleotide bindingi2222 – 22298ATP Reviewed prediction
Nucleotide bindingi2593 – 26008ATP Reviewed prediction
Nucleotide bindingi2935 – 29428ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: InterPro
  3. microtubule motor activity Source: InterPro
  4. protein binding Source: HGNC
Complete GO annotation...

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 – 11Removed By similarity
Chaini2 – 46444643Cytoplasmic dynein 1 heavy chain 1
PRO_0000114629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei1123 – 11231N6-acetyllysine By similarity
Modified residuei3478 – 34781N6-acetyllysine By similarity
Modified residuei4281 – 42811N6-acetyllysine By 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 18651864Stem By similarity
Add
BLAST
Regioni446 – 701256Interaction with DYNC1I2
Add
BLAST
Regioni649 – 800152Interaction with DYNC1LI2
Add
BLAST
Regioni1866 – 2097232AAA 1 By similarity
Add
BLAST
Regioni2178 – 2450273AAA 2 By similarity
Add
BLAST
Regioni2554 – 2803250AAA 3 By similarity
Add
BLAST
Regioni2897 – 3166270AAA 4 By similarity
Add
BLAST
Regioni3187 – 3498312Stalk By similarity
Add
BLAST
Regioni3551 – 3780230AAA 5 By similarity
Add
BLAST
Regioni4003 – 4219217AAA 6 By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili48 – 6922 Reviewed prediction
Add
BLAST
Coiled coili179 – 20022 Reviewed prediction
Add
BLAST
Coiled coili453 – 47624 Reviewed prediction
Add
BLAST
Coiled coili541 – 56424 Reviewed prediction
Add
BLAST
Coiled coili1169 – 120133 Reviewed prediction
Add
BLAST
Coiled coili1229 – 125022 Reviewed prediction
Add
BLAST
Coiled coili1355 – 137117 Reviewed prediction
Add
BLAST
Coiled coili3187 – 327387 Reviewed prediction
Add
BLAST
Coiled coili3394 – 3498105 Reviewed prediction
Add
BLAST
Coiled coili3735 – 379864 Reviewed prediction
Add
BLAST

Domaini

Dynein heavy chains probably consist of an N-terminal stem (which binds cargo and interacts with other dynein components), and the head or motor domain. The motor contains six tandemly-linked AAA domains in the head, which form a ring. A stalk-like structure (formed by two of the coiled coil domains) protrudes between AAA 4 and AAA 5 and terminates in a microtubule-binding site. A seventh domain may also contribute to this ring; it is not clear whether the N-terminus or the C-terminus forms this extra domain. There are four well-conserved and two non-conserved ATPase sites, one per AAA domain. Probably only one of these (within AAA 1) actually hydrolyzes ATP, the others may serve a regulatory function.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5245.
HOGENOMiHOG000176055.
HOVERGENiHBG096595.
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

« Hide

MSETGGGEDG SAGLEVSAVQ NVADVSVLQK HLRKLVPLLL EDGGDAPAAL     50
EAALEEKSAL EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN 100
INIDIHYGVK SNSLAFIKRA PVIDADKPVS SQLRVLTLSE DSPYETLHSF 150
ISNAVAPFFK SYIRESGKAD RDGDKMAPSV EKKIAELEMG LLHLQQNIEI 200
PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL NQLQSGVNRW 250
IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD 300
ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK 350
IRQALVAIFT HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM 400
HVAYEEFEKV MVACFEVFQT WDDEYEKLQV LLRDIVKRKR EENLKMVWRI 450
NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR VLRPQVTAVA QQNQGEAPEP 500
QDMKVAEVLF DAADANAIEE VNLAYENVKE VDGLDVSKEG TEAWEAAMKR 550
YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR 600
EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK 650
QIDRQLTAYM KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW 700
ARKVQQRNLG VSGRIFTIES ARVRGRSGNV LKLKVNFLPE IITLSKEVRN 750
LKWLGFRVPL AIVNKAHQAN QLYPFAISLI ESVRTYERTC EKVEERNTIS 800
LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN FQEKVDDLLI 850
IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK 900
LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE 950
PKIKNVVHEL RITNQVIYLN PPIEECRYKL YQEMFAWKMI VLSLPRIQSQ 1000
RYQVGVHYEL TEEEKFYRNA LTRSRDGPVA LEESYSAVMG IVTEVEQYVK 1050
VWLQYQCLWD MQAENIYNRL GEDLSKWQAL LVQIRRARGT FDNAETKKEF 1100
GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF HSQISKSRQE 1150
LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF 1200
QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES 1250
RTTDLLTDWE KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE 1300
ALELTDTGLL SGSEERVQVA LEELQDLKGV WSELSKVWEQ IDQMKEQPWV 1350
SVQPRKLRQN LDGLLNQLKN FPARLRQYAS YEFVQRLLKG YMKINMLVIE 1400
LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN EAIVKDVLLV 1450
AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN 1500
SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT 1550
GSADIKHLLP VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE 1600
RLADLLGKIQ KALGEYLERE RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK 1650
HFKKMFAGVS SIILNEDSSV VLGISSREGE EVMFKTPVSI TEHPKINEWL 1700
TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI DKYQAQLVVL 1750
SAQIAWSENV ENALSNVGGG GNVGPLQSVL SNVEVTLNVL ADSVLMEQPP 1800
LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD 1850
VLQQLSIQMA NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG 1900
SPFGPAGTGK TESVKALGHQ LGRFVLVFNC DETFDFQAMG RIFVGLCQVG 1950
AWGCFDEFNR LEERMLSAVS QQVQCIQEAL REHSNPNYDK TSAPITCELL 2000
NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT KPDRQLIAQV 2050
MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSPGN 2100
VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSFC ETMVPKLVAE 2150
DIPLLFSLLS DVFPGVQYHR GEMTDLREEL KKVCKEMYLT YGDGEEVGGM 2200
WVEKVLQLYQ ITQINHGLMM VGPSGSGKSM AWRVLLKALE RLEGVEGVAH 2250
IIDPKAISKD HLYGTLDPNT REWTDGLFTH VLRKIIDNVR GELQKRQWIV 2300
FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM FEVQDLKYAT 2350
LATVSRCGMV WFSEDLLSTD MIFNNFLARL RTIPLDEGED EAQRRRKGKE 2400
DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL 2450
RCLGSLFSML HQGCRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL 2500
SGDSRLKMRA ELGEYIRRIT TVPLPTAPNI PIIDYEVSIS GEWSPWQAKV 2550
PQIEVETHKV AAPDVVVPTL DTVRHEALLY TWLAEHKPLV LCGPPGSGKT 2600
MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR RTPNGVVLAP 2650
VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGGF YRTSDQTWVK 2700
LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN 2750
RAMLRLIPSL RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW 2800
VRGIFEALRP LETLPVEGLI RIWAHEALRL FQDRLVEDEE RRWTDENIDM 2850
VALKHFPNID KEKAMSRPIL YSNWLSKDYI PVDQEELRDY VKARLKVFYE 2900
EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG KTTLSRFVAW 2950
MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS 3000
GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK 3050
WFTSQVIRNL HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL 3100
YQVGKEFTSK MDLEKPNYIV PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ 3150
TLHQANARLA KRGGRTMAIT PRHYLDFINH YANLFHEKRS ELEEQQMHLN 3200
VGLRKIKETV DQVEELRRAL RIKSQELEVK NAAANDKLKK MVKDQQEAEK 3250
KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ 3300
HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV 3350
NFSAEEISDA IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY 3400
ADMLKRVEPL RNELQKLEDD AKDNQQKANE VEQMIRDLEA SIARYKEEYA 3450
VLISEAQAIK ADLAAVEAKV NRSTALLKSL SAERERWEKT SETFKNQMST 3500
IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ FRTDIARTEY 3550
LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN 3600
EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE 3650
VRRTGGRVLI TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT 3700
VTRSSLQSQC LNEVLKAERP DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA 3750
LNEVKGRILD DDTIITTLEN LKREAAEVTR KVEETDIVMQ EVETVSQQYL 3800
PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE NPNLKGATDH 3850
TQRLSVITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTMGEPTYD 3900
AEFQHFLRGK EIVLSAGSTP KVQGLTVEQA EAVARLSCLP AFKDLIAKVQ 3950
ADEQFGIWLE SSSPEQTVPY LWTEETPATP IGQAIHRLLL IQAFRPDRLL 4000
AMAHMFVSTN LGESFMSIME QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS 4050
GHVEDLAAEQ NTQITSIAIG SAEGFNQADK AINTAVKSGR WVMLKNVHLA 4100
PGWLMQLEKK LHSLQPHACF RLFLTMEINP RVPVNLLRAG RIFVFEPPPG 4150
VKANMLRTFS SIPVSRMCKS PNERARLYFL LAWFHAVIQE RLRYAPLGWS 4200
KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY 4250
GGRVDNEFDQ RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR 4300
EEFVQWVELL PDAQTPSWLG LPNNAERVLL TTQGVDMISK MLKMQMLEDE 4350
DDLAYAETEK KTRTDFTSDG RPAWMRTLHT TASNWLHLIP QTLSPLKRTV 4400
ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK KQTNYLRTLI 4450
NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAAAGGAK 4500
ELKNIHVCLG ALFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSTT 4550
LDACSFGVTG LKLQGATCSN NKLSLSNAIS TVLPLTQLRW GKQTSAEKKA 4600
SVVTLPVYLN FTRADLIFTV DFEIATKEDP RSFYERGVAV LCTE 4644
Length:4,644
Mass (Da):532,252
Last modified:February 1, 1995 - v1
Checksum:i8C6ABDBEDF875D82
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1024 – 10252SR → MP in AAA41103. 1 Publication
Sequence conflicti1772 – 17721N → D in AAA41103. 1 Publication
Sequence conflicti2098 – 20981P → A in AAA41103. 1 Publication
Sequence conflicti2139 – 21391F → V in AAA41103. 1 Publication
Sequence conflicti2175 – 21751D → A in AAA41103. 1 Publication
Sequence conflicti2185 – 21851K → Q in AAA41103. 1 Publication
Sequence conflicti2366 – 23661L → V in AAA41103. 1 Publication
Sequence conflicti2382 – 23821T → S in AAA41103. 1 Publication
Sequence conflicti2463 – 24631G → A in AAA41103. 1 Publication
Sequence conflicti3219 – 32191A → D in AAA41103. 1 Publication
Sequence conflicti4131 – 41311R → K in AAA41103. 1 Publication
Sequence conflicti4366 – 43661F → S in AAA41103. 1 Publication
Sequence conflicti4511 – 45111A → G in AAA41103. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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...

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: June 11, 2014
This is version 123 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

Similar proteinsi