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P36022 (DYHC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynein heavy chain, cytoplasmic
Alternative name(s):
Dynein heavy chain, cytosolic
Short name=DYHC
Gene names
Name:DYN1
Synonyms:DHC1
Ordered Locus Names:YKR054C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length4092 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytoplasmic dynein 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. Required to maintain uniform nuclear distribution in hyphae. May play an important role in the proper orientation of the mitotic spindle into the budding daughter cell yeast. Probably required for normal progression of the cell cycle. Ref.7

Subunit structure

The dynein complex consists of at least two heavy chains and a number of intermediate and light chains. Interacts with DYN3. Ref.7

Subcellular location

Cytoplasmcytoskeleton. Note: Concentrates at motile dots in the cytoplasm corresponding to the plus ends of cytoplasmic microtubules. Ref.5 Ref.7

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.

Miscellaneous

Present with 195 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the dynein heavy chain family.

Ontologies

Keywords
   Biological processKaryogamy
   Cellular componentCytoplasm
Cytoskeleton
Dynein
Microtubule
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processestablishment of mitotic spindle localization

Inferred from mutant phenotype PubMed 21633107. Source: SGD

establishment of mitotic spindle orientation

Inferred from mutant phenotype PubMed 9281582. Source: SGD

karyogamy

Inferred from electronic annotation. Source: UniProtKB-KW

metabolic process

Inferred from direct assay PubMed 16873064. Source: GOC

mitotic sister chromatid segregation

Inferred from genetic interaction PubMed 7860634. Source: SGD

nuclear migration along microtubule

Inferred from mutant phenotype PubMed 9201714. Source: SGD

   Cellular_componentastral microtubule

Inferred from direct assay PubMed 16580990. Source: SGD

cell cortex

Inferred from direct assay Ref.7. Source: SGD

cytoplasmic dynein complex

Inferred from physical interaction PubMed 9658168. Source: SGD

cytoplasmic microtubule

Inferred from direct assay PubMed 12566428PubMed 15965467. Source: SGD

spindle pole body

Inferred from direct assay PubMed 16580990. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from electronic annotation. Source: InterPro

microtubule motor activity

Inferred from direct assay PubMed 16873064. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMC1P329083EBI-6230,EBI-17402

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 40924092Dynein heavy chain, cytoplasmic
PRO_0000114643

Regions

Nucleotide binding1796 – 18038ATP Potential
Nucleotide binding2074 – 20818ATP Potential
Nucleotide binding2418 – 24258ATP Potential
Nucleotide binding2760 – 27678ATP Potential
Region1 – 17571757Stem By similarity
Region1758 – 1979222AAA 1 By similarity
Region2036 – 2273238AAA 2 By similarity
Region2379 – 2628250AAA 3 By similarity
Region2722 – 2984263AAA 4 By similarity
Region2993 – 3300308Stalk By similarity
Region3370 – 3599230AAA 5 By similarity
Region3760 – 3970211AAA 6 By similarity
Coiled coil154 – 17522 Potential
Coiled coil486 – 50823 Potential
Coiled coil542 – 56625 Potential
Coiled coil932 – 95928 Potential
Coiled coil1042 – 106322 Potential
Coiled coil1681 – 170525 Potential
Coiled coil2993 – 3092100 Potential
Coiled coil3242 – 330059 Potential
Coiled coil3532 – 360877 Potential

Experimental info

Sequence conflict5891Y → C in AAA16055. Ref.4
Sequence conflict6011V → A in AAA16055. Ref.4
Sequence conflict13641E → A in AAA16055. Ref.4
Sequence conflict2118 – 21192ML → IV in CAA79923. Ref.1

Secondary structure

..................................................................................................................................................................................................................................................................................................................................................................... 4092
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36022 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 3D9DF447E8E2D6BB

FASTA4,092471,348
        10         20         30         40         50         60 
MCKNEARLAN ELIEFVAATV TGIKNSPKEN EQAFIDYLHC QYLERFQFFL GLLDGREFDT 

        70         80         90        100        110        120 
LFVFLFEELD RTIVTIDIGE EAIYDANLAN KKYSTLLIIK SRSVIVDAEP IATQISAIYL 

       130        140        150        160        170        180 
PGPVNAGNLA SIITHGVSSV FGQLIKSDTK TYSVETIDKT RRKLDDISKQ FQQLHTSIET 

       190        200        210        220        230        240 
PDLLAMVPSI IKLAVSKGAT SHDYANYLPS NDLESMRFLN ILQSIANKWF LVLKQTLAID 

       250        260        270        280        290        300 
RDIKNGSFLD EVEFWSNFYE VLKSLIEQTQ SQEFQVCLSV LTNAKRFHNL TNLLNEGSLS 

       310        320        330        340        350        360 
DKFKLADKYN QFLSSIPIDE VRQASNLEDL QELFPVLASS LKKFRYSGYP VQRFVVLMDK 

       370        380        390        400        410        420 
ISQEVMDAIL SNLSDLFQLE YGSFLGLYEK SAGMIEEWDD IVQDVNLLIR EDLRKRAPQE 

       430        440        450        460        470        480 
LLIQKLTFTS ASVKATLDEI LSTRKRFFSL AETIKSISPS TYHEEIQRLY HPFEQIHDIS 

       490        500        510        520        530        540 
VNFRLKLEQA ESEFSKNMLD LEKKLQNTLA SFMDSDHCPT EKLSYLVKFK PLMELCPRIK 

       550        560        570        580        590        600 
VKVLENQQIL LLEIKKDIRQ LETGLELLPK ILHVEALNNI PPISARISYF LNVQSRIDNI 

       610        620        630        640        650        660 
VQYLEALFGS NWNDTLEGRS ISTSIVQLRK ETNPHDVFLH WLGNFPEKAT ANLLTTPILK 

       670        680        690        700        710        720 
LIRNNEDDYE LKVNFDFALA AAYSELRSLT YMAFQVPSHI VRIARTYMYL YPRAINLVEL 

       730        740        750        760        770        780 
IQTFFSLSKS LSYTFYTNIF LKRNVQTVWL LLQQILITPW ESLQEESSEM SCSVHSLARL 

       790        800        810        820        830        840 
EKSIDGILSD YQILKNSEPQ FAKEFSGLKS FDGTADDLHE VEEIISNIQA IFENLFTKGL 

       850        860        870        880        890        900 
TNVSDHISTF NNLIISIILE KVRLNLKKMH FPKHVLKLSF NEGRITSSPS LAAMKRSLLK 

       910        920        930        940        950        960 
DIEALLNKVV LINFLHDPDH PLSTTLTFNS LVIKLKDDIQ NCIEQVQNLH CKINSYVKEW 

       970        980        990       1000       1010       1020 
QKMEFLWQIT EEAFLEVVDN STQRCFGILK GLLDSQSKFD LIISRNNFSK NLVLHTEDAQ 

      1030       1040       1050       1060       1070       1080 
RHIRSKMDSW ILYVSKHLLT IYERDARKLH EDMNRDREAV EDMDINFTSL KNITVIIEAV 

      1090       1100       1110       1120       1130       1140 
NVNKRHLTER DIQIKLLGSV MRALTKLKVR FPSHFVYIDQ LDNDFSSLRQ SLSYVEQELQ 

      1150       1160       1170       1180       1190       1200 
KHRVVIAKSL EEGVENINNL SQSLNESWSV RKPISPTLTP PEALKILEFF NESITKLKKK 

      1210       1220       1230       1240       1250       1260 
MHSVAAAAKM LLIPVVLNDQ LTHVVEEVKT YDLVWRSIKN LWEDVQRTFE TPWCRVDVLL 

      1270       1280       1290       1300       1310       1320 
LQSDLANFLR RADELPRAVK QFEMYKSLFS QVNMLTSVNK ILVELKDGAL KPRHWNMIFR 

      1330       1340       1350       1360       1370       1380 
DIGKRQIQKN LLDKLEFSLK DVMVLNLTLN EILLTKIIER AQKEFVIEKS LNRIKKFWKE 

      1390       1400       1410       1420       1430       1440 
AQYEVIEHSS GLKLVREWDV LEQACKEDLE ELVSMKASNY YKIFEQDCLD LESKLTKLSE 

      1450       1460       1470       1480       1490       1500 
IQVNWVEVQF YWLDLYGILG ENLDIQNFLP LETSKFKSLT SEYKMITTRA FQLDTTIEVI 

      1510       1520       1530       1540       1550       1560 
HIPNFDTTLK LTIDSLKMIK SSLSTFLERQ RRQFPRFYFL GNDDLLKIIG SGKHHDQVSK 

      1570       1580       1590       1600       1610       1620 
FMKKMFGSIE SIIFLEDFIT GVRSVEGEVL NLNEKIELKD SIQAQEWLNI LDTEIKLSVF 

      1630       1640       1650       1660       1670       1680 
TQFRDCLGQL KDGTDIEVVV SKYIFQAILL SAQVMWTELV EKCLQTNQFS KYWKEVDMKI 

      1690       1700       1710       1720       1730       1740 
KGLLDKLNKS SDNVKKKIEA LLVEYLHFNN VIGQLKNCST KEEARLLWAK VQKFYQKNDT 

      1750       1760       1770       1780       1790       1800 
LDDLNSVFIS QSGYLLQYKF EYIGIPERLI YTPLLLIGFA TLTDSLHQKY GGCFFGPAGT 

      1810       1820       1830       1840       1850       1860 
GKTETVKAFG QNLGRVVVVF NCDDSFDYQV LSRLLVGITQ IGAWGCFDEF NRLDEKVLSA 

      1870       1880       1890       1900       1910       1920 
VSANIQQIQN GLQVGKSHIT LLEEETPLSP HTAVFITLNP GYNGRSELPE NLKKSFREFS 

      1930       1940       1950       1960       1970       1980 
MKSPQSGTIA EMILQIMGFE DSKSLASKIV HFLELLSSKC SSMNHYHFGL RTLKGVLRNC 

      1990       2000       2010       2020       2030       2040 
SPLISEFGEG EKTVVESLKR VILPSLGDTD ELVFKDELSK IFDSAGTPLN SKAIVQCLKD 

      2050       2060       2070       2080       2090       2100 
AGQRSGFSMS EEFLKKCMQF YYMQKTQQAL ILVGKAGCGK TATWKTVIDA MAIFDGHANV 

      2110       2120       2130       2140       2150       2160 
VYVIDTKVLT KESLYGSMLK ATLEWRDGLF TSILRRVNDD ITGTFKNSRI WVVFDSDLDP 

      2170       2180       2190       2200       2210       2220 
EYVEAMNSVL DDNKILTLPN GERLPIPPNF RILFETDNLD HTTPATITRC GLLWFSTDVC 

      2230       2240       2250       2260       2270       2280 
SISSKIDHLL NKSYEALDNK LSMFELDKLK DLISDSFDMA SLTNIFTCSN DLVHILGVRT 

      2290       2300       2310       2320       2330       2340 
FNKLETAVQL AVHLISSYRQ WFQNLDDKSL KDVITLLIKR SLLYALAGDS TGESQRAFIQ 

      2350       2360       2370       2380       2390       2400 
TINTYFGHDS QELSDYSTIV IANDKLSFSS FCSEIPSVSL EAHEVMRPDI VIPTIDTIKH 

      2410       2420       2430       2440       2450       2460 
EKIFYDLLNS KRGIILCGPP GSGKTMIMNN ALRNSSLYDV VGINFSKDTT TEHILSALHR 

      2470       2480       2490       2500       2510       2520 
HTNYVTTSKG LTLLPKSDIK NLVLFCDEIN LPKLDKYGSQ NVVLFLRQLM EKQGFWKTPE 

      2530       2540       2550       2560       2570       2580 
NKWVTIERIH IVGACNPPTD PGRIPMSERF TRHAAILYLG YPSGKSLSQI YEIYYKAIFK 

      2590       2600       2610       2620       2630       2640 
LVPEFRSYTE PFARASVHLY NECKARYSTG LQSHYLFSPR ELTRLVRGVY TAINTGPRQT 

      2650       2660       2670       2680       2690       2700 
LRSLIRLWAY EAWRIFADRL VGVKEKNSFE QLLYETVDKY LPNQDLGNIS STSLLFSGLL 

      2710       2720       2730       2740       2750       2760 
SLDFKEVNKT DLVNFIEERF KTFCDEELEV PMVIHESMVD HILRIDRALK QVQGHMMLIG 

      2770       2780       2790       2800       2810       2820 
ASRTGKTILT RFVAWLNGLK IVQPKIHRHS NLSDFDMILK KAISDCSLKE SRTCLIIDES 

      2830       2840       2850       2860       2870       2880 
NILETAFLER MNTLLANADI PDLFQGEEYD KLLNNLRNKT RSLGLLLDTE QELYDWFVGE 

      2890       2900       2910       2920       2930       2940 
IAKNLHVVFT ICDPTNNKSS AMISSPALFN RCIINWMGDW DTKTMSQVAN NMVDVIPMEF 

      2950       2960       2970       2980       2990       3000 
TDFIVPEVNK ELVFTEPIQT IRDAVVNILI HFDRNFYQKM KVGVNPRSPG YFIDGLRALV 

      3010       3020       3030       3040       3050       3060 
KLVTAKYQDL QENQRFVNVG LEKLNESVLK VNELNKTLSK KSTELTEKEK EARSTLDKML 

      3070       3080       3090       3100       3110       3120 
MEQNESERKQ EATEEIKKIL KVQEEDIRKR KEVVMKSIQD IEPTILEAQR GVKNIKKQQL 

      3130       3140       3150       3160       3170       3180 
TEIRSMVNPP SGVKIVMEAV CAILGYQFSN WRDIQQFIRK DDFIHNIVHY DTTLHMKPQI 

      3190       3200       3210       3220       3230       3240 
RKYMEEEFLS DPNFTYETIN RASKACGPLY QWVNAQINFS KVLENVDPLR QEMKRIEFES 

      3250       3260       3270       3280       3290       3300 
LKTKANLLAA EEMTQDLEAS IEVSKRKYSL LIRDVEAIKT EMSNVQANLD RSISLVKSLT 

      3310       3320       3330       3340       3350       3360 
FEKERWLNTT KQFSKTSQEL IGNCIISSIY ETYFGHLNER ERADMLVILK RLLGKFAVKY 

      3370       3380       3390       3400       3410       3420 
DVNYRFIDYL VTLDEKMKWL ECGLDKNDYF LENMSIVMNS QDAVPFLLDP SSHMITVISN 

      3430       3440       3450       3460       3470       3480 
YYGNKTVLLS FLEEGFVKRL ENAIRFGSVV IIQDGEFFDP IISRLISREF NHAGNRVTVE 

      3490       3500       3510       3520       3530       3540 
IGDHEVDVSG DFKLFIHSCD PSGDIPIFLR SRVRLVHFVT NKESIETRIF DITLTEENAE 

      3550       3560       3570       3580       3590       3600 
MQRKREDLIK LNTEYKLKLK NLEKRLLEEL NNSQGNMLEN DELMVTLNNL KKEAMNIEKK 

      3610       3620       3630       3640       3650       3660 
LSESEEFFPQ FDNLVEEYSI IGKHSVKIFS MLEKFGQFHW FYGISIGQFL SCFKRVFIKK 

      3670       3680       3690       3700       3710       3720 
SRETRAARTR VDEILWLLYQ EVYCQFSTAL DKKFKMIMAM TMFCLYKFDI ESEQYKEAVL 

      3730       3740       3750       3760       3770       3780 
TMIGVLSESS DGVPKLTVDT NNDLRYLWDY VTTKSYISAL NWFKNEFFVD EWNIADVVAN 

      3790       3800       3810       3820       3830       3840 
SENNYFTMAS ERDVDGTFKL IELAKASKES LKIIPLGSIE NLNYAQEEIS KSKIEGGWIL 

      3850       3860       3870       3880       3890       3900 
LQNIQMSLSW VKTYLHKHVE ETKAAEEHEK FKMFMTCHLT GDKLPAPLLQ RTDRFVYEDI 

      3910       3920       3930       3940       3950       3960 
PGILDTVKDL WGSQFFTGKI SGVWSVYCTF LLSWFHALIT ARTRLVPHGF SKKYYFNDCD 

      3970       3980       3990       4000       4010       4020 
FQFASVYLEN VLATNSTNNI PWAQVRDHIA TIVYGGKIDE EKDLEVVAKL CAHVFCGSDN 

      4030       4040       4050       4060       4070       4080 
LQIVPGVRIP QPLLQQSEEE ERARLTAILS NTIEPADSLS SWLQLPRESI LNYERLQAKE 

      4090 
VASSTEQLLQ EM 

« Hide

References

« Hide 'large scale' references
[1]"Cytoplasmic dynein is required for normal nuclear segregation in yeast."
Eshel D., Urrestarazu L.A., Vissers S., Jauniaux J.-C., van Vliet-Reedijk J.C., Planta R.J., Gibbons I.R.
Proc. Natl. Acad. Sci. U.S.A. 90:11172-11176(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Disruption of mitotic spindle orientation in a yeast dynein mutant."
Li Y.-Y., Yeh E.Y., Hays T., Bloom K.S.
Proc. Natl. Acad. Sci. U.S.A. 90:10096-10100(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-3457.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"The offloading model for dynein function: differential function of motor subunits."
Lee W.-L., Kaiser M.A., Cooper J.A.
J. Cell Biol. 168:201-207(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DYN3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21877 Genomic DNA. Translation: CAA79923.1.
L15626 Unassigned DNA. Translation: AAA16055.1.
Z28279 Genomic DNA. Translation: CAA82132.1.
BK006944 Genomic DNA. Translation: DAA09205.1.
PIRS38128.
RefSeqNP_012980.1. NM_001179844.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QMZX-ray6.00A/B1364-4092[»]
4AI6X-ray3.40A/B1364-4092[»]
4AKGX-ray3.30A/B1364-4092[»]
4AKHX-ray3.60A/B1364-4092[»]
4AKIX-ray3.70A/B1364-4092[»]
ProteinModelPortalP36022.
SMRP36022. Positions 1793-1857, 2067-2092, 2187-2217, 2412-2628, 2750-2820, 3045-3254, 3257-3653.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34185. 224 interactions.
DIPDIP-2644N.
IntActP36022. 9 interactions.
MINTMINT-427451.
STRING4932.YKR054C.

Proteomic databases

PaxDbP36022.
PRIDEP36022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR054C; YKR054C; YKR054C.
GeneID853928.
KEGGsce:YKR054C.

Organism-specific databases

CYGDYKR054c.
SGDS000001762. DYN1.

Phylogenomic databases

eggNOGCOG5245.
GeneTreeENSGT00750000117443.
HOGENOMHOG000176055.
KOK10413.
OMAEMWITKA.
OrthoDBEOG7MH16D.

Enzyme and pathway databases

BioCycYEAST:G3O-32023-MONOMER.

Gene expression databases

GenevestigatorP36022.

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. 3 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 5 hits.
ProtoNetSearch...

Other

NextBio975291.
PROP36022.

Entry information

Entry nameDYHC_YEAST
AccessionPrimary (citable) accession number: P36022
Secondary accession number(s): D6VXB5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references