UniProtKB - P36022 (DYHC_YEAST)
Protein
Dynein heavy chain, cytoplasmic
Gene
DYN1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
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.1 Publication
Miscellaneous
Present with 195 molecules/cell in log phase SD medium.1 Publication
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Nucleotide bindingi | 1796 – 1803 | ATPSequence analysis | 8 | |
| Nucleotide bindingi | 2074 – 2081 | ATPSequence analysis | 8 | |
| Nucleotide bindingi | 2418 – 2425 | ATPSequence analysis | 8 | |
| Nucleotide bindingi | 2760 – 2767 | ATPSequence analysis | 8 |
GO - Molecular functioni
- ATP binding Source: SGD
- ATP-dependent microtubule motor activity, minus-end-directed Source: SGD
- dynein intermediate chain binding Source: GO_Central
- dynein light chain binding Source: GO_Central
- dynein light intermediate chain binding Source: GO_Central
GO - Biological processi
- cytoplasmic microtubule organization Source: GO_Central
- establishment of mitotic spindle localization Source: SGD
- establishment of mitotic spindle orientation Source: SGD
- karyogamy Source: UniProtKB-KW
- minus-end-directed vesicle transport along microtubule Source: GO_Central
- mitotic sister chromatid segregation Source: SGD
- nuclear migration along microtubule Source: SGD
Keywordsi
| Molecular function | Motor protein |
| Biological process | Karyogamy |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
| BioCyci | YEAST:G3O-32023-MONOMER |
Names & Taxonomyi
| Protein namesi | Recommended name: Dynein heavy chain, cytoplasmicAlternative name(s): Dynein heavy chain, cytosolic Short name: DYHC |
| Gene namesi | Name:DYN1 Synonyms:DHC1 Ordered Locus Names:YKR054C |
| Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic identifieri | 559292 [NCBI] |
| Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
| Proteomesi |
|
Organism-specific databases
| EuPathDBi | FungiDB:YKR054C |
| SGDi | S000001762 DYN1 |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000114643 | 1 – 4092 | Dynein heavy chain, cytoplasmicAdd BLAST | 4092 |
Proteomic databases
| MaxQBi | P36022 |
| PaxDbi | P36022 |
| PRIDEi | P36022 |
PTM databases
| iPTMneti | P36022 |
Interactioni
Subunit structurei
The dynein complex consists of at least two heavy chains and a number of intermediate and light chains. Interacts with DYN3.1 Publication
Binary interactionsi
GO - Molecular functioni
- dynein intermediate chain binding Source: GO_Central
- dynein light chain binding Source: GO_Central
- dynein light intermediate chain binding Source: GO_Central
Protein-protein interaction databases
| BioGridi | 34185, 347 interactors |
| ComplexPortali | CPX-1178 Cytoplasmic dynein complex |
| DIPi | DIP-2644N |
| IntActi | P36022, 11 interactors |
| MINTi | P36022 |
| STRINGi | 4932.YKR054C |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
| ProteinModelPortali | P36022 |
| SMRi | P36022 |
| ModBasei | Search... |
| MobiDBi | Search... |
Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Regioni | 1 – 1757 | StemBy similarityAdd BLAST | 1757 | |
| Regioni | 1758 – 1979 | AAA 1By similarityAdd BLAST | 222 | |
| Regioni | 2036 – 2273 | AAA 2By similarityAdd BLAST | 238 | |
| Regioni | 2379 – 2628 | AAA 3By similarityAdd BLAST | 250 | |
| Regioni | 2722 – 2984 | AAA 4By similarityAdd BLAST | 263 | |
| Regioni | 2993 – 3300 | StalkBy similarityAdd BLAST | 308 | |
| Regioni | 3370 – 3599 | AAA 5By similarityAdd BLAST | 230 | |
| Regioni | 3760 – 3970 | AAA 6By similarityAdd BLAST | 211 |
Coiled coil
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Coiled coili | 154 – 175 | Sequence analysisAdd BLAST | 22 | |
| Coiled coili | 486 – 508 | Sequence analysisAdd BLAST | 23 | |
| Coiled coili | 542 – 566 | Sequence analysisAdd BLAST | 25 | |
| Coiled coili | 932 – 959 | Sequence analysisAdd BLAST | 28 | |
| Coiled coili | 1042 – 1063 | Sequence analysisAdd BLAST | 22 | |
| Coiled coili | 1681 – 1705 | Sequence analysisAdd BLAST | 25 | |
| Coiled coili | 2993 – 3092 | Sequence analysisAdd BLAST | 100 | |
| Coiled coili | 3242 – 3300 | Sequence analysisAdd BLAST | 59 | |
| Coiled coili | 3532 – 3608 | Sequence analysisAdd BLAST | 77 |
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, RepeatPhylogenomic databases
| GeneTreei | ENSGT00910000144015 |
| HOGENOMi | HOG000176055 |
| InParanoidi | P36022 |
| KOi | K10413 |
| OMAi | QKRQWII |
| OrthoDBi | EOG092C00NZ |
Family and domain databases
| InterProi | View protein in InterPro IPR003593 AAA+_ATPase IPR035699 AAA_6 IPR011704 ATPase_dyneun-rel_AAA IPR035706 DHC_D5 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 |
| PANTHERi | PTHR10676 PTHR10676, 1 hit |
| Pfami | View protein in Pfam PF07728 AAA_5, 1 hit PF12774 AAA_6, 1 hit PF12780 AAA_8, 1 hit PF12781 AAA_9, 1 hit PF08385 DHC_N1, 1 hit PF08393 DHC_N2, 1 hit PF03028 Dynein_heavy, 1 hit PF12777 MT, 1 hit |
| SMARTi | View protein in SMART SM00382 AAA, 3 hits |
| SUPFAMi | SSF52540 SSF52540, 5 hits |
Sequencei
Sequence statusi: Complete.
P36022-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MCKNEARLAN ELIEFVAATV TGIKNSPKEN EQAFIDYLHC QYLERFQFFL
60 70 80 90 100
GLLDGREFDT LFVFLFEELD RTIVTIDIGE EAIYDANLAN KKYSTLLIIK
110 120 130 140 150
SRSVIVDAEP IATQISAIYL PGPVNAGNLA SIITHGVSSV FGQLIKSDTK
160 170 180 190 200
TYSVETIDKT RRKLDDISKQ FQQLHTSIET PDLLAMVPSI IKLAVSKGAT
210 220 230 240 250
SHDYANYLPS NDLESMRFLN ILQSIANKWF LVLKQTLAID RDIKNGSFLD
260 270 280 290 300
EVEFWSNFYE VLKSLIEQTQ SQEFQVCLSV LTNAKRFHNL TNLLNEGSLS
310 320 330 340 350
DKFKLADKYN QFLSSIPIDE VRQASNLEDL QELFPVLASS LKKFRYSGYP
360 370 380 390 400
VQRFVVLMDK ISQEVMDAIL SNLSDLFQLE YGSFLGLYEK SAGMIEEWDD
410 420 430 440 450
IVQDVNLLIR EDLRKRAPQE LLIQKLTFTS ASVKATLDEI LSTRKRFFSL
460 470 480 490 500
AETIKSISPS TYHEEIQRLY HPFEQIHDIS VNFRLKLEQA ESEFSKNMLD
510 520 530 540 550
LEKKLQNTLA SFMDSDHCPT EKLSYLVKFK PLMELCPRIK VKVLENQQIL
560 570 580 590 600
LLEIKKDIRQ LETGLELLPK ILHVEALNNI PPISARISYF LNVQSRIDNI
610 620 630 640 650
VQYLEALFGS NWNDTLEGRS ISTSIVQLRK ETNPHDVFLH WLGNFPEKAT
660 670 680 690 700
ANLLTTPILK LIRNNEDDYE LKVNFDFALA AAYSELRSLT YMAFQVPSHI
710 720 730 740 750
VRIARTYMYL YPRAINLVEL IQTFFSLSKS LSYTFYTNIF LKRNVQTVWL
760 770 780 790 800
LLQQILITPW ESLQEESSEM SCSVHSLARL EKSIDGILSD YQILKNSEPQ
810 820 830 840 850
FAKEFSGLKS FDGTADDLHE VEEIISNIQA IFENLFTKGL TNVSDHISTF
860 870 880 890 900
NNLIISIILE KVRLNLKKMH FPKHVLKLSF NEGRITSSPS LAAMKRSLLK
910 920 930 940 950
DIEALLNKVV LINFLHDPDH PLSTTLTFNS LVIKLKDDIQ NCIEQVQNLH
960 970 980 990 1000
CKINSYVKEW QKMEFLWQIT EEAFLEVVDN STQRCFGILK GLLDSQSKFD
1010 1020 1030 1040 1050
LIISRNNFSK NLVLHTEDAQ RHIRSKMDSW ILYVSKHLLT IYERDARKLH
1060 1070 1080 1090 1100
EDMNRDREAV EDMDINFTSL KNITVIIEAV NVNKRHLTER DIQIKLLGSV
1110 1120 1130 1140 1150
MRALTKLKVR FPSHFVYIDQ LDNDFSSLRQ SLSYVEQELQ KHRVVIAKSL
1160 1170 1180 1190 1200
EEGVENINNL SQSLNESWSV RKPISPTLTP PEALKILEFF NESITKLKKK
1210 1220 1230 1240 1250
MHSVAAAAKM LLIPVVLNDQ LTHVVEEVKT YDLVWRSIKN LWEDVQRTFE
1260 1270 1280 1290 1300
TPWCRVDVLL LQSDLANFLR RADELPRAVK QFEMYKSLFS QVNMLTSVNK
1310 1320 1330 1340 1350
ILVELKDGAL KPRHWNMIFR DIGKRQIQKN LLDKLEFSLK DVMVLNLTLN
1360 1370 1380 1390 1400
EILLTKIIER AQKEFVIEKS LNRIKKFWKE AQYEVIEHSS GLKLVREWDV
1410 1420 1430 1440 1450
LEQACKEDLE ELVSMKASNY YKIFEQDCLD LESKLTKLSE IQVNWVEVQF
1460 1470 1480 1490 1500
YWLDLYGILG ENLDIQNFLP LETSKFKSLT SEYKMITTRA FQLDTTIEVI
1510 1520 1530 1540 1550
HIPNFDTTLK LTIDSLKMIK SSLSTFLERQ RRQFPRFYFL GNDDLLKIIG
1560 1570 1580 1590 1600
SGKHHDQVSK FMKKMFGSIE SIIFLEDFIT GVRSVEGEVL NLNEKIELKD
1610 1620 1630 1640 1650
SIQAQEWLNI LDTEIKLSVF TQFRDCLGQL KDGTDIEVVV SKYIFQAILL
1660 1670 1680 1690 1700
SAQVMWTELV EKCLQTNQFS KYWKEVDMKI KGLLDKLNKS SDNVKKKIEA
1710 1720 1730 1740 1750
LLVEYLHFNN VIGQLKNCST KEEARLLWAK VQKFYQKNDT LDDLNSVFIS
1760 1770 1780 1790 1800
QSGYLLQYKF EYIGIPERLI YTPLLLIGFA TLTDSLHQKY GGCFFGPAGT
1810 1820 1830 1840 1850
GKTETVKAFG QNLGRVVVVF NCDDSFDYQV LSRLLVGITQ IGAWGCFDEF
1860 1870 1880 1890 1900
NRLDEKVLSA VSANIQQIQN GLQVGKSHIT LLEEETPLSP HTAVFITLNP
1910 1920 1930 1940 1950
GYNGRSELPE NLKKSFREFS MKSPQSGTIA EMILQIMGFE DSKSLASKIV
1960 1970 1980 1990 2000
HFLELLSSKC SSMNHYHFGL RTLKGVLRNC SPLISEFGEG EKTVVESLKR
2010 2020 2030 2040 2050
VILPSLGDTD ELVFKDELSK IFDSAGTPLN SKAIVQCLKD AGQRSGFSMS
2060 2070 2080 2090 2100
EEFLKKCMQF YYMQKTQQAL ILVGKAGCGK TATWKTVIDA MAIFDGHANV
2110 2120 2130 2140 2150
VYVIDTKVLT KESLYGSMLK ATLEWRDGLF TSILRRVNDD ITGTFKNSRI
2160 2170 2180 2190 2200
WVVFDSDLDP EYVEAMNSVL DDNKILTLPN GERLPIPPNF RILFETDNLD
2210 2220 2230 2240 2250
HTTPATITRC GLLWFSTDVC SISSKIDHLL NKSYEALDNK LSMFELDKLK
2260 2270 2280 2290 2300
DLISDSFDMA SLTNIFTCSN DLVHILGVRT FNKLETAVQL AVHLISSYRQ
2310 2320 2330 2340 2350
WFQNLDDKSL KDVITLLIKR SLLYALAGDS TGESQRAFIQ TINTYFGHDS
2360 2370 2380 2390 2400
QELSDYSTIV IANDKLSFSS FCSEIPSVSL EAHEVMRPDI VIPTIDTIKH
2410 2420 2430 2440 2450
EKIFYDLLNS KRGIILCGPP GSGKTMIMNN ALRNSSLYDV VGINFSKDTT
2460 2470 2480 2490 2500
TEHILSALHR HTNYVTTSKG LTLLPKSDIK NLVLFCDEIN LPKLDKYGSQ
2510 2520 2530 2540 2550
NVVLFLRQLM EKQGFWKTPE NKWVTIERIH IVGACNPPTD PGRIPMSERF
2560 2570 2580 2590 2600
TRHAAILYLG YPSGKSLSQI YEIYYKAIFK LVPEFRSYTE PFARASVHLY
2610 2620 2630 2640 2650
NECKARYSTG LQSHYLFSPR ELTRLVRGVY TAINTGPRQT LRSLIRLWAY
2660 2670 2680 2690 2700
EAWRIFADRL VGVKEKNSFE QLLYETVDKY LPNQDLGNIS STSLLFSGLL
2710 2720 2730 2740 2750
SLDFKEVNKT DLVNFIEERF KTFCDEELEV PMVIHESMVD HILRIDRALK
2760 2770 2780 2790 2800
QVQGHMMLIG ASRTGKTILT RFVAWLNGLK IVQPKIHRHS NLSDFDMILK
2810 2820 2830 2840 2850
KAISDCSLKE SRTCLIIDES NILETAFLER MNTLLANADI PDLFQGEEYD
2860 2870 2880 2890 2900
KLLNNLRNKT RSLGLLLDTE QELYDWFVGE IAKNLHVVFT ICDPTNNKSS
2910 2920 2930 2940 2950
AMISSPALFN RCIINWMGDW DTKTMSQVAN NMVDVIPMEF TDFIVPEVNK
2960 2970 2980 2990 3000
ELVFTEPIQT IRDAVVNILI HFDRNFYQKM KVGVNPRSPG YFIDGLRALV
3010 3020 3030 3040 3050
KLVTAKYQDL QENQRFVNVG LEKLNESVLK VNELNKTLSK KSTELTEKEK
3060 3070 3080 3090 3100
EARSTLDKML MEQNESERKQ EATEEIKKIL KVQEEDIRKR KEVVMKSIQD
3110 3120 3130 3140 3150
IEPTILEAQR GVKNIKKQQL TEIRSMVNPP SGVKIVMEAV CAILGYQFSN
3160 3170 3180 3190 3200
WRDIQQFIRK DDFIHNIVHY DTTLHMKPQI RKYMEEEFLS DPNFTYETIN
3210 3220 3230 3240 3250
RASKACGPLY QWVNAQINFS KVLENVDPLR QEMKRIEFES LKTKANLLAA
3260 3270 3280 3290 3300
EEMTQDLEAS IEVSKRKYSL LIRDVEAIKT EMSNVQANLD RSISLVKSLT
3310 3320 3330 3340 3350
FEKERWLNTT KQFSKTSQEL IGNCIISSIY ETYFGHLNER ERADMLVILK
3360 3370 3380 3390 3400
RLLGKFAVKY DVNYRFIDYL VTLDEKMKWL ECGLDKNDYF LENMSIVMNS
3410 3420 3430 3440 3450
QDAVPFLLDP SSHMITVISN YYGNKTVLLS FLEEGFVKRL ENAIRFGSVV
3460 3470 3480 3490 3500
IIQDGEFFDP IISRLISREF NHAGNRVTVE IGDHEVDVSG DFKLFIHSCD
3510 3520 3530 3540 3550
PSGDIPIFLR SRVRLVHFVT NKESIETRIF DITLTEENAE MQRKREDLIK
3560 3570 3580 3590 3600
LNTEYKLKLK NLEKRLLEEL NNSQGNMLEN DELMVTLNNL KKEAMNIEKK
3610 3620 3630 3640 3650
LSESEEFFPQ FDNLVEEYSI IGKHSVKIFS MLEKFGQFHW FYGISIGQFL
3660 3670 3680 3690 3700
SCFKRVFIKK SRETRAARTR VDEILWLLYQ EVYCQFSTAL DKKFKMIMAM
3710 3720 3730 3740 3750
TMFCLYKFDI ESEQYKEAVL TMIGVLSESS DGVPKLTVDT NNDLRYLWDY
3760 3770 3780 3790 3800
VTTKSYISAL NWFKNEFFVD EWNIADVVAN SENNYFTMAS ERDVDGTFKL
3810 3820 3830 3840 3850
IELAKASKES LKIIPLGSIE NLNYAQEEIS KSKIEGGWIL LQNIQMSLSW
3860 3870 3880 3890 3900
VKTYLHKHVE ETKAAEEHEK FKMFMTCHLT GDKLPAPLLQ RTDRFVYEDI
3910 3920 3930 3940 3950
PGILDTVKDL WGSQFFTGKI SGVWSVYCTF LLSWFHALIT ARTRLVPHGF
3960 3970 3980 3990 4000
SKKYYFNDCD FQFASVYLEN VLATNSTNNI PWAQVRDHIA TIVYGGKIDE
4010 4020 4030 4040 4050
EKDLEVVAKL CAHVFCGSDN LQIVPGVRIP QPLLQQSEEE ERARLTAILS
4060 4070 4080 4090
NTIEPADSLS SWLQLPRESI LNYERLQAKE VASSTEQLLQ EM
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 589 | Y → C in AAA16055 (PubMed:8234262).Curated | 1 | |
| Sequence conflicti | 601 | V → A in AAA16055 (PubMed:8234262).Curated | 1 | |
| Sequence conflicti | 1364 | E → A in AAA16055 (PubMed:8234262).Curated | 1 | |
| Sequence conflicti | 2118 – 2119 | ML → IV in CAA79923 (PubMed:8248224).Curated | 2 |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z21877 Genomic DNA Translation: CAA79923.1 L15626 Unassigned DNA Translation: AAA16055.1 Z28279 Genomic DNA Translation: CAA82132.1 BK006944 Genomic DNA Translation: DAA09205.1 |
| PIRi | S38128 |
| RefSeqi | NP_012980.1, NM_001179844.1 |
Genome annotation databases
| EnsemblFungii | YKR054C; YKR054C; YKR054C |
| GeneIDi | 853928 |
| KEGGi | sce:YKR054C |
Similar proteinsi
Entry informationi
| Entry namei | DYHC_YEAST | |
| Accessioni | P36022Primary (citable) accession number: P36022 Secondary accession number(s): D6VXB5 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
| Last sequence update: | June 1, 1994 | |
| Last modified: | September 12, 2018 | |
| This is version 163 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Fungal Protein Annotation Program | |



